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(dT)12 + UTP
diphosphate + ?
-
assay uses poly(A) as an RNA template and oligo(dT)12-18 as the primer. Enzyme is strictly dependent on the presence of primer
-
-
?
2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
5-fluorouridine triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme incorporates 5-fluorouridine monophosphate during RNA elongation in place of UMP or CMP using homopolymeric and heteropolymeric templates. Incorporation of 5-fluorouridine monophosphate does not prevent chain elongation, and, in some sequence contexts, it favors misincorporations at downstream positions. 5-Fluorouridine monophosphate is incorporated into the nascent RNA and occupies the new 3'-end of the primer at the active site of the enzyme. 5-Fluorouridine monophosphate establishes a Watson and Crick pair with the corresponding acceptor AMP in the template strand and an additional hydrogen bond with Ser304 of the polymerase. Further interactions, similar to those observed with standard nucleotides, contribute also to stabilize 5-fluorouridine monophosphate in the 3'-terminus of the RNA. When present in the template, 5-fluorouridine monophosphate directs the incorporation of AMP and GMP, with ATP being a more effective substrate than GTP. The misincorporation of GMP is 17fold faster opposite 5-fluorouridine than opposite U in the template. But Incorporated 5-fluorouridine monophosphate is not a chain terminator during RNA elongation
RNA with incoporated 5-fluorouridine phosphate
-
?
ara-ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + poly(U)
diphosphate + ?
ATP + RNAn
diphosphate + RNAn+1
ATP + sshRNAn
diphosphate + sshRNAn+1
-
-
-
-
?
CTP + RNA9
diphosphate + RNA10
AJ242654
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
CTP + sshRNAn
diphosphate + sshRNAn+1
-
-
-
-
?
dATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
GTP + poly(C)
diphosphate + ?
GTP + poly(C)
diphosphate + poly(C)n+1
-
-
-
-
?
GTP + poly(C)n
diphosphate + poly(C)n+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
GTP + sshRNAn
diphosphate + sshRNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
remdesivir triphosphate + RNAn
diphosphate + RNAn+1
remdesivir triphosphate is effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
-
-
?
rGTP + RNAn
diphosphate + RNAn+1
ribavirin triphosphate + RNAn
?
ribavirin is a guanosine analogue that can be a substrate for the viral RNA polymerase. HCV is genetically variable, and this genetic variation can affect the polymerase's use of ribavirin triphosphate, overview
-
-
?
UTP + poly(A)n
diphosphate + poly(A)n+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
UTP + sshRNAn
diphosphate + sshRNAn+1
-
-
-
-
?
additional information
?
-
ATP + poly(U)
diphosphate + ?
-
-
-
-
?
ATP + poly(U)
diphosphate + ?
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
ir
CTP + RNAn
diphosphate + RNAn+1
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
?
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
GTP + RNAn
diphosphate + RNAn+1
with poly(rC)
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
full-length negative strand BBV RNAs are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is active in an in vitro RNA polymerase assay using homopolymeric RNA or BVDV minigenomic RNA templates. The major product is a covalently linked double-stranded molecule. In addition, a nucleotide-nonspecific and template-independent terminal nucleotidyl transferase activity is observed
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
dependent on and specific for BMV RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAs of Brome mosaic virus and the closely related cowpea Chlorotic mottle virus are the most effective, but some activity is also shown by certain other viral nucleic acids and polyribonucleotides
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is completely dependent on exogenous template. The enzyme utilizes a variety of viral RNAs and CMV satellite RNA as template for minus-strand synthesis. Cellular RNAs are not used as templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme copies CMV RNA and several other viral RNAs, Brome mosaic virus RNA, Alfalfa mosaic virus RNA and Tobacco mosaic virus RNA. Activity with poly(C) and poly(U) but not poly(A) or poly(G). The product with CMV RNA as template is heterogenous in size with a peak length of about 150 residues
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP + CMV RNA, yeast RNA or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
the polymerase structure is switchable, with a discrete set of contacts stabilizing the initiation-competent form of the enzyme so that relatively modest changes can have-range effects, controlling the switch from the initiation to elongation phase, with premature conformational switching producing a structure that preferentially initiates by back-priming
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
template is RNA, the phi6 polymerase is highly processive and can use either single- or double-stranded RNA as a template and synthesizes a full-length complementary strand of an RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
NTPs are ATP, GTP, CTP, and UTP, roles of the negatively charged plough area on the polymerase surface, of the rim of the template tunnel and of the template specificity pocket that is key in the formation of the productive RNA-polymerase binary complex. The positively charged rim of the template tunnel has a significant role in the engagement of highly structured ssRNA molecules, whereas specific interactions further down in the template tunnel promote ssRNA entry to the catalytic site
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
homopolymer C as the template and biotinoligo(G)20 as the primer
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
using homopolymer C as the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
enzyme initiates RNA synthesis in a primer- and poly(A)-dependent manner in vitro
product is double-stranded RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme does not manifest strict specificity towards EMC RNA template. It can use also Qbeta RNA, rRNA of BHK cells or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
catalysis and translocation are uncoupled in the viral RNA-dependent RNA polymerase. A motif B loop may assist the movement of the template strand in late stages of transcription
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A)-dependent oligo(U)-primed poly(U) polymerase activity. In the presence of an oligo(U) primer, the enzyme catalyzes the synthesis of a full-length copy of either poliovirus or globin RNA templates. In the absence of added primer, RNA products up to twice the length of the template are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic mechanism for single nucleotide incorporation catalyzed by poliovirus polymerase in presence of Mg2+
-
-
r
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RdRP incorporation of incorrect nucleosides is inefficient, making precise determination of kinetic parameters experimentally challenging. The fidelity for poliovirus polymerase 3Dpol ranges from 12000 to 1000000 for transition mutations and 32000 to 43000000 for transversion mutations
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
VPg (a peptide comprising the 3B region of protein 3AB) is the 22-residue soluble product of 3AB cleavage and serves as the protein primer for RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
substrate is HP1 RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
purified recombinant FMDV 3D is active in polymerization assays using homopolymeric and heteropolymeric primer templates and in binding to RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Foxtail mosaic potexvirus
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ATP, the enzyme requires a single-stranded molecule of RNA or polyribonucleotide as template, initiates new chains with purine ribonucleoside triphosphates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
661081, 662733, 673227, 690468, 690470, 690615, 691255, 691257, 691273, 692029, 693537, 695258, 737570, 738678, 738870, 759501 -
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
polyC/oligoG is more efficient in supporting the HCV NS5B polymerase activity than polyA/oligodT. PolyA/oligoU or polyI/oligodC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme performs RNA- or DNA oligonucleotide primer-dependent RNA synthesis on templates with a blocked 3' end or on homopolymeric templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ribonucleotide-incorporating activity on an in vitro transcribed RNA containing the 3' end of the HCV genome. It also possesses ribunucleotide incorporation activity, to a lesser extent, on in vitro transcribed foreign RNA templates when RNA or DNA primers are present. The activity is higher with DNA primers than with RNA primers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA-dependent RNA polymerase activity uses poly(C) most efficiently as a template but is inactive on poly(U) and poly(G). The enzyme is able to copy a full-length or nearly full-length genome in the absence of additional viral or cellular cofactors. Poly(C)-oligo(G)12 is the most efficient substrate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
once synthesis has begun, the C-terminally truncated enzyme NS5B(DELTA21) does not dissociate from the template until a complete double strand copy of the RNA is made
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication of Hepatitits C virus is thought to proceed via the initial synthesis of a complementary (-)RNA strand, which serves, in turn, as a template for the production of progeny (+)-strand RNA molecules. An RNA-dependent RNA polymerase is postulated to be involved in these steps
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
essential catalytic enzyme for HCV replication. NS5A binds RNA-dependent RNA polymerase and modulates RNA-dependent RNA polymerase activity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
poly(C) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
nculeotides are GTP, CTP, ATP, and UTP, the RNA templates for the enzyme assay are transcribed from linearized murine inducible nitric oxide synthase, iNOS, clone having 400 nt insert in an in vitro transcription reaction using SP6 RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II. Extension of B2 RNA by Pol II occurs from the 3'-end and is internally templated and requires all four NTPs, mechanism, overview. No activity with B2 RNA mutated at C155 to G
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription using the model RNA template, v84
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication occurs through de novo initiation and involves a complementary RNA intermediate
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the NS5 protein is able to use both plus- and minus-strand 3'-untranslated regions of the JEV genome as templates in the absence of a primer, with the latter RNA being a better template. Analysis of the RNA synthesis initiation site using the 3'-end 83 nucleotides of the JEV genome as a minimal RNA template reveals that the NS5 protein specifically initiates RNA synthesis from an internal site, U81, at the two nucleotides upstream of the 3'-end of the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
La France isometric virus
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
La France isometric virus
-
the enzyme is probably a transcriptase engaged in the synthesis of ssRNA transcripts corresponding to each of the virion-associated dsRNAs
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the polymerase product anneals only to measles RNA and not to Vero cell RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
viral ribonucleoprotein complexes and purified recombinant L protein but not P protein exhibit mRNA (guanine-7-)methyl-transferase activity. mRNA synthesis in a reconstituted transcription system using purified N protein-genomic RNA complex as a template requires both the L and P proteins. Enzymatic properties of Senda virus mRNA (guanine-7-)methyl-transferase are different to that of cellular mRNA (guanine-7-)methyl-transferase. Unlike cellular enzyme, the SeV enzyme preferentially methylates capped RNA containing the viral mRNA 5'-end sequences (GpppApGpG-). The C-terminal part (amino acid residues 1,7562,228) of the L protein catalyzes cap methylation, whereas the N-terminal half (residues 11,120) containing putative RNA polymerase subdomains does not
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the random polymers poly(UG), poly(UC), poly(AG) and poly(AU) serve as more effective templates than homopolymers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NV 3Dpol yields two different products when incubated with synthetic RNA in vitro: (1) a double-stranded RNA consisting of two single strands of opposite polarity or (2) the single-stranded RNA template labelled at its 39 terminus by terminal transferase activity. Initiation of RNA synthesis by NV 3Dpol on heteromeric RNA template occurs de novo
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
when the nucleotide concentrations are low, C is incorporated at the fastest rate and G at the slowest. G-incorporation step largely limits the overall reaction rate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Qbeta replicase is an RNA-dependent RNA polymerase responsible for replicating the RNA genome of coliphage Qbeta and plays a key role in the life cycle of the Qbeta phage
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic model for the RNA replication reaction
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme (RdRP) is essential for both transcription and replication of the viral RNA genome
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in presence of Mg2+ significant activity is observed when poly(A) or poly(C) is used as template and the activity is template and primer-dependent. Poly(G) and poly(U) templates are not efficient substrates. Biotinylated oligoDNA primers appear to work slightly more efficiently than oligoRNA primers. In presence of Mn2+ activity is stimulated 2.5-5.6fold. RNA synthesis using poly(C) as template becomes primer-independent
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA polymerase activity on homopolymeric templates poly(A) and poly(C) and heteropolymeric RNA templates primed with either RNA or DNA oligonucleotide primers or self-primed by a copy-back mechanism
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in a synthetic RNA template-dependent reaction, sapovirus 3Dpol synthesizes a double-stranded RNA or labels the template 3' terminus by terminal transferase activity. Initiation of RNA synthesis occurs de novo on heteropolymeric templates or in a primer dependent manner on polyadenylated templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
essential enzyme for viral RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
key enzyme responsible for the SARS-CoV-2 replication process, catalyzes the synthesis of complementary minus strand RNA and genomic plus strand RNA. Identification of potential key agents for targeting RNA-dependent RNA polymerase of SARS-CoV-2 by integrated analysis and virtual drug screening
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
RNA-dependent RNA polymerase is a key enzyme which regulates the viral replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plas a key role in the replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plays a crucial role in SARS-CoV-2 replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the nsp12 (RdRp) is a central component of SARS-CoV-2 replication/transcription machinery. It catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
cryo-EM structures of the SARS-CoV-2 RNA polymerase in complexes with RNA, before and after RNA translocation, reveals structural rearrangements that the RNA-dependent RNA polymerase (RdRp) nsp12 and its co-factors (nsp7 and nsp8) undergo to accommodate nucleic acid binding
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
SARS-CoV-2 core polymerase complex has less efficient activity for RNA synthesis and lower thermostability of individual subunits compared with SARSCoV
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nsP4 possesses the RNA-dependent RNA polymerase activity required for the replication of the SIN genome and transcription of a subgenomic mRNA during infection
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in the absence of other viral proteins nsP4 is capable of copying SIN plus- and minus-strand templates, but does not transcribe subgenomic RNA. Mutations in the 3' conserved sequence element and poly(A) tail of the plus-strand template prevent nsP4-mediated de novo initiation of minus-strand RNA synthesis. nsP4-dependent terminal addition of nucleotides occurs on template RNA possessing certain mutations in the 3' conserved sequence element and polyadenylate tail. nsP4 is capable of minus-strand synthesis independent of the sequence at the 5' end of the template. An A-U rich sequence in the 3' conserved sequence element represents a binding site for a replicase component. Probably nsP4 plus-strand genomic RNA synthesis is dependent on the 3' end of the minus-strand template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes in vitro the transcription of short single-stranded RNA and DNA molecules into precise complementary RNA copies up to the full length of these templates. The transcription of RNA-oligonicleotide templates and DNA-oligonucleotide templates is equally effective. Differences in transcription efficiency are found to depend on nucleotide sequence rather than on the RNA or DNA nature of the single-stranded nucleic acid. Double-stranded nucleic acids such as poly(A)*poly(U) and a double-stranded DNA 14-mer are not transcribed. The RdRP-directed transcription can be primed. The unprimed transcription starts preferentially at the 3'-terminal nucleotide of the template. The enzyme is capable of adding a single noncomplementary nucleotide to the 3'-terminus of about 50% of the runoff transcripts. AMP is preferred over GMP whereas CMP and UMP are terminally added at very low frequency
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key step in the reproduction of plus-stranded RNA viruses pathogens is replication of their single-stranded RNA genomes occuring in the cytosol of host cells in association with membranes and requiring a virally-encoded RNA-dependent RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is able to synthesize or finish full-length TNV-RNA on an endogenous template, the minus strand of TNV-RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
both 5'- and 3'-terminal regions of the (+)-strand RNA template including the wild type cyclization motifs are important for RNA synthesis. However, the 3'-terminal region of the (-)-strand RNA template alone is sufficient for RNA synthesis. The (+)-strand 5'-cyclization motif is critical for (-)-strand RNA synthesis but neither the (-)-strand 5'- nor 3'-cyclization motif is important for the (+)-strand RNA synthesis. Cyclization of the viral RNA play a role for (-)-strand RNA synthesis but not for (+)-strand RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
DNA can serve as a template for ZIKV NS5 with an efficiency similar to that of an RNA template. The enzyme (NS5) can utilize single-stranded DNA but not double-stranded DNA as a template or a primer to synthesize RNA. Both full-length NS5 and a truncated NS5 containing the polymerase domain can carry out in vitro RNA-dependent RNA synthesis
-
-
?
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
rGTP + RNAn
diphosphate + RNAn+1
-
-
-
?
rGTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
ir
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
additional information
?
-
-
the central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity
-
-
?
additional information
?
-
-
introns called mirtrons and sirtrons might serve as the single-stranded RNA precursors for the generation of microRNA and small interfering RNA (siRNA), respectively, through an RDR (RNA-dependent RNA polymerase)-dependent pathway. sRNA high-throughput sequencing in wild-type and RDR-deficient mutant plants, overview
-
-
?
additional information
?
-
-
introns called mirtrons and sirtrons might serve as the single-stranded RNA precursors for the generation of microRNA and small interfering RNA (siRNA), respectively, through an RDR (RNA-dependent RNA polymerase)-dependent pathway. sRNA high-throughput sequencing in wild-type and RDR-deficient mutant plants, overview
-
-
?
additional information
?
-
-
the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
-
-
?
additional information
?
-
-
systemic necrotic spotting induced by ORMV in tobacco maps to the RdRp polymerase domain, comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
?
additional information
?
-
Cystovirus phi6
-
construction of a Coxsackie virus B3-specific GFP siRNA pool
-
-
?
additional information
?
-
Cystovirus phi6
-
In silico template RNA modelling, overview
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
D-elp1, corresponding to the largest of the three subunits in the RNA polymerase II core elongator complex, has RNA-dependent RNA polymerase activity. RdRP activity is associated with the amino terminal 96-kD fragment, DELTAC, CDS 1-2528. D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA templates using either a primer-dependent or primer-independent initiation mechanism, overview. D-elp1 associates tightly with Dcr-2
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
interaction of EV71 3Dpol and the nuclear protein U5 snRNPs. ENzyme 3Dpol enters the cellular nucleus and colocalizes with pre-mRNA processing factor 8, Prp8, 3Dpol associates with the C-terminal domain of Prp8 containing the Jab1/MPN region. RIP-seq of the pre-mRNA are trapped by the Prp8-3Dpol complexes
-
-
?
additional information
?
-
-
viral RdRP elongation nucleotide addition cycle (NAC), structure-function analysis, overview
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
interaction of EV71 3Dpol and the nuclear protein U5 snRNPs. ENzyme 3Dpol enters the cellular nucleus and colocalizes with pre-mRNA processing factor 8, Prp8, 3Dpol associates with the C-terminal domain of Prp8 containing the Jab1/MPN region. RIP-seq of the pre-mRNA are trapped by the Prp8-3Dpol complexes
-
-
?
additional information
?
-
-
the conservative lysine residue K359 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
-
-
?
additional information
?
-
-
in vitro, protein nsp9 of equine arteritis virus shows weak de novo polymerase activity on homopolymeric RNA templates. The RNA-synthesizing activities observed in de novo and primer-dependent polymerase and terminal transferase assays cannot be attributed to recombinant EAV nsp9-RdRp. The polymerase assay employing 32P-labeled NTPs is sensitive enough to detect the activity of trace amounts of contaminating T7 RNA polymerase. This polymerase is also able to act on templates lacking the established T7 promoter requirements
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additional information
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enzyme-host membrane interactions are an initial step of FHV RNA replication complex assembly, overview
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additional information
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the enzyme translates in vitro rapidly. It specifically associates with mitochondria isolated from yeast, insect, and mammalian cells, temperature-dependently but independent of protease-sensitive mitochondrial outer membrane components or the host mitochondrial import machinery. The enzyme preferentially binds to specific anionic phospholipids, in particular the mitochondrion-specific phospholipid cardiolipin
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additional information
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the initiation of FMDV RNA synthesis is strongly inhibited by 5-fluorouridine triphosphate, and it is also an inhibitor of FMDV RNA elongation, overview
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additional information
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the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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the viral enzyme binds to its coding region RNA stem-loop structure, 5BSL3.2, and its negative strand, enzyme and RNA interaction is an important step in viral RNA replication, overview
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additional information
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presence of motif G is important for primer-dependent RNA synthesis but not to affect the binding of the enzyme to the template
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additional information
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the viral enzyme binds to its coding region RNA stem-loop structure, 5BSL3.2, and its negative strand, enzyme and RNA interaction is an important step in viral RNA replication, overview
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additional information
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RNA polymerase II (PolII) acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Pol II extends B2 RNA by 18 nt on its 3'-end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
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additional information
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the heterotrimeric complex of PB1, PB2 and PA subunits cooperate in the transcription and replication of the viral genome, the N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding and RNA polymerase activity as well as virulence of the strains, overview
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additional information
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the polymerase protein also harbors an intrinsic RNA and DNA endonuclease activity that cleaves host mRNAs during cap-snatching, inhibited by 2,4-dioxo-4-phenylbutanoic and activated by Mn2+, with the amino-terminal 209 residues of the PA subunit containing the endonuclease active site, structure-function analysis, overview
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additional information
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the RdRp catalyzes all the biochemical reactions of influenza virus transcription and replication in vitro, dinucleotide ApG and globin mRNA-primed transcription, de novo initiation/replication, and polyadenylation
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additional information
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the polymerase protein also harbors an intrinsic RNA and DNA endonuclease activity that cleaves host mRNAs during cap-snatching, inhibited by 2,4-dioxo-4-phenylbutanoic and activated by Mn2+, with the amino-terminal 209 residues of the PA subunit containing the endonuclease active site, structure-function analysis, overview
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
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flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
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additional information
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flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
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additional information
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ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
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additional information
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ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
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flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
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additional information
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ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
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additional information
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the RNA-dependent RNA polymerase of arenaviruses is an integral part of the L protein, a 200-kDa multifunctional and multidomain protein, structure and function of the Lassa virus RdRp domain, folding model of thedomain, overview
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additional information
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residues K1127, R1134, E1135, L1136, D1140, and K1144, D1193, G1298, S1333, D1334, D1335, and K1376 from different subunits might be involved in catalysis
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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pseudogene-derived antisense siRNAs can be produced in specific rice developmental stages or physiological growth conditions, suggesting their potentially important roles in normal rice development involving RDR2, or small RNAs from rice pseudogenes might also function as natural antisense siRNAs either by interacting with the complementary sense RNAs from functional parental genes or by forming double-strand RNAs with transcripts of adjacent paralogous pseudogenes, function classification of rice pseudogenes, overview
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additional information
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Potato spindle tuber viroid replication in the nucleoplasm generates (-)-PSTVd intermediates and (+)-PSTVd copies. The Nicotiana benthamiana canonical 9-zinc finger (ZF) transcription factor IIIA (TFIIIA-9ZF) as well as its variant TFIIIA-7ZF both interact with (+)-PSTVd, but only TFIIIA-7ZF interacts with (-)-PSTVd. TFIIIA-7ZF is found in the nucleoplasm and nucleolus, in contrast to the strictly nucleolar localization of TFIIIA-9ZF. The DNA-dependent RNA polymerase II interacts with the (+)- and (2)-PSTVd RNA in vivo
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additional information
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template ssRNA accesses the active site through a tunnel. The phi12 P2 conformation does not favor RNA binding
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additional information
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RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
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additional information
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RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
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additional information
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RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
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additional information
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the C-terminal fragment can interact with the viral nucleocapsid protein, the N-terminal 50 amino acids of nucleocapsid protein are responsible for the NP-RdRp interaction
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
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enzyme shows both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. It preferentially copies homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer and is also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of human SARS coronavirus, using the 3'-terminal 36- and 37-nt RNA, respectively
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additional information
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enzyme shows both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. It preferentially copies homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer and is also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of human SARS coronavirus, using the 3'-terminal 36- and 37-nt RNA, respectively
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additional information
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comparison of necrotic lesions of wild-type and chimeric mutant virusses
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additional information
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The single-stranded RNA genomes of the plus-stranded RNA viruses serve as templates for translation of viral proteins and perform other essential functions that generally involve local RNA structures, such as RNA hairpins. Viral RNA replication also requires a long-range RNA-RNA interaction
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
?
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
?
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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additional information
?
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formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
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(1R)-6-bromo-N-[(1S)-1-phenylethyl]-2,3,4,9-tetrahydro-1H-carbazol-1-amine
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(1S)-1-(4-aminofuro[3,2-d]pyrimidin-7-yl)-1,4-anhydro-2-C-methyl-D-ribitol
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(1S)-1-(4-aminothieno[3,2-d]pyrimidin-7-yl)-1,4-anhydro-2-C-methyl-D-ribitol
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(2E)-3-(4-[[(1-[[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]amino]cyclobutyl)carbonyl]amino]phenyl)prop-2-enoic acid
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(2E)-3-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)prop-2-enoic acid
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(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2E)-3-[4-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-2-azido-2-[[(2-methylpropanoyl)oxy]methyl]tetrahydrofuran-3,4-diyl bis(2-methylpropanoate)
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(2R,3S,5S)-5-(methoxycarbonyl)-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
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(2R,3S,5S)-5-[(aminooxy)carbonyl]-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
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(2S)-(((5Z)-5-[(5-ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)amino)(4-fluorophenyl)acetic acid
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(2S)-1-[(2-amino-4-chloro-5-methylphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
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(2S)-1-[(3,4,5-trichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
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(2S)-1-[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
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(2S)-1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]pyrrolidine-2-carboxylic acid
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(2S)-2-[(2,4-dichlorobenzoyl)(3-nitrobenzyl)amino]-3-phenylpropanoic acid
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(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-thiophen-2-ylpyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-2-isobutyl-4-(2-phenylacetyl)-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2-carboxylic acid
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(2S,4S,5R)-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-4-acetyl-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2-carboxylic acid
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(2S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-2,5-dihydro-1H-pyrrole-2,4-dicarboxylic acid
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(2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
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(2Z)-2-(benzoylamino)-3-[4-(2-bromophenoxy)phenyl]acrylic acid
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(2Z)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(2Z)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
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(4E)-1-(3,4-dimethylphenyl)-4-(hydroxyimino)pyrazolidine-3,5-dione
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(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-[[(2-phenylethoxy)sulfinyl]carbamoyl]-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-thiophen-2-yl-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-2-(2-methylpropyl)-4-[(2-phenylethyl)carbamoyl]-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-4-[[(trifluoromethoxy)sulfinyl]carbamoyl]-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-(benzylcarbamoyl)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-4-(ethylcarbamoyl)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(1-methylethyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[[(benzyloxy)sulfinyl]carbamoyl]-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(5,7-difluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
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(5,8-dicyano-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
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(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
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(5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
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(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
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(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
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(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(5S)-5-tert-butyl-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)-1,5-dihydro-2H-pyrrol-2-one
-
-
(6R,7R,8S,9R)-4-bromo-7,8-dihydroxy-7,8,9,10-tetrahydro-5H,6H-6,9-epoxy-1,2,5a,10a-tetraazacycloocta[1,2,3-cd]inden-5-one
-
-
([[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]oxy]methyl)phosphonic acid
-
-
1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
-
moderate antiproliferative activity for the cell lines tested
1,3-dimethyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
1-(1-methylethyl)-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
1-(2,5-difluorophenyl)-3-phenyltriazene
1-(2,5-difluorophenyl)azopyrrolidine
1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
1-(3-bromophenyl)azopiperidine
1-(3-bromophenyl)azopyrrolidine
1-(3-chloro)-3-phenyltriazene N-methyl
1-(3-chlorophenyl)azopiperidine
1-(3-chlorophenyl)azopyrrolidine
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
1-(3-nitrophenyl)-3-phenyltriazene
1-(3-nitrophenyl)azopiperidine
1-(3-nitrophenyl)azopyrrolidine
1-(3-trifluoromethylphenyl)azopyrrolidine
1-(4-bromophenyl)azopiperidine
1-(4-bromophenyl)azopyrrolidine
1-(4-chlorophenyl)azopiperidine
1-(4-chlorophenyl)azopyrrolidine
1-(4-methoxyphenyl)azopyrrolidine
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
1-(4-nitrophenyl)azopyrrolidine
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
-
-
1-benzyl-N-(2,3-dimethylphenyl)-3,5-dimethyl-1H-pyrazole-4-carboxamide
NIC04, in combination with NIC02, i.e. N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboximidic acid
1-benzyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-(3-oxomorpholin-4-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-hydroxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-methylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-methoxy-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopiperidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(3-furyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[4-(dimethylcarbamoyl)phenyl](phenyl)methoxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[5-(1,1-dioxidoisothiazolidin-2-yl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[5-(dimethylcarbamoyl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1H-benzimidazole-5-carboxamide
-
-
1-cyclohexyl-2-phenyl-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-phenyl-1H-indole-5-carboxylic acid
-
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(1-methylethyl)carbamoyl]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(methoxyacetyl)(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-[2-fluoro-4-[(2-morpholin-4-ylbenzyl)oxy]phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-pyridin-2-yl-1H-benzimidazole-5-carboxamide
-
-
1-ethyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-3-(trifluoromethyl)-N-[4-(pyrrolidinylsulfonyl)-phenyl]-1H-pyrazole-5-carboxamide
-
specific inhibitor, inhibits RdRp complex activity
1-methyl-3-(trifluoromethyl)-N-[4-(pyrrolidinylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
1-methyl-3-(trifluoromethyl)-N-[4-pyrrolidinylsulfonylphenyl]-1H-pyrazole-5-carboxamide
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
1-methyl-4-(phenylazo)piperazine
1-methyl-4-(trifluoromethyl)-N-(4-[[4-(trifluoromethyl)piperidin-1-yl]sulfonyl]phenyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-5-[[4-(pyrrolidin-1-ylsulfonyl)phenoxy]methyl]-3-(trifluoromethyl)-1H-pyrazole
-
-
1-methyl-N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(morpholin-4-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(piperazin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(piperazin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
first-in-class nonnucleoside inhibitor of RNA-dependent RNA polymerase complex activity, highly active against multiple primary isolates of diverse measles virus genotypes circulating worldwide, high developmental potential as a potent therapeutic against measles virus, active concentrations of 35-145 nM
1-methyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-[(4-methylpiperidin-1-yl)sulfonyl]phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
1-phenyl-3-benzyltriazene
1-phenyl-3-methyl-3-benzyltriazene
1-phenyl-3-phenyltriazene
1-phenyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-phenylazo-4-oxopiperidine
1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-[(2-chlorophenyl)carbamoyl]-2-(1,3-thiazol-4-ylmethyl)piperazine-2-carboxylic acid
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
1-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-2-[4-(pyrrolidin-1-ylsulfonyl)phenyl]ethanol
-
-
1-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-2-[4-(pyrrolidin-1-ylsulfonyl)phenyl]ethanone
-
-
1-[2-(diethylamino)ethyl]-6-(1H-imidazol-1-yl)-1,3-dihydro-2H-benzimidazol-2-one
-
1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboxylic acid
-
-
1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-3-carboxylic acid
-
-
1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]proline
-
-
12-cyclohexylindolo[1,2-c][1,3]benzoxazine-9-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 24°
13-cyclohexyl-3-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
13-cyclohexyl-5-(2-piperidin-1-ylethyl)-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
-
-
13-cyclohexyl-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 46°
13-cyclohexyl-6,7-dihydro-5H-indolo[2,1-a][2]benzazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 53°
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzothiazepine-10-carboxylate
-
dihedral angle between the C2-aryl group and the indole ring is 56°
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 43°
14-cyclohexyl-7,8-dihydro-6H-indolo[1,2-e][1,5]benzoxazocine-11-carboxylate
-
dihedral angle between the C2-aryl group and the indole ring is 61°
1H-benzimidazole-5-carboxylic acid, 2-[4-[[4'-chloro-4-(2-oxo-1-pyrrolidinyl)[1,1'-biphenyl]-2-yl]methoxy]-2-fluorophenyl]-1-cyclohexyl hydrochloride
i.e. JTK-109
2',3'-dideoxycytidine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2',3'-dideoxyguanosine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-C-ethynyl-2'-fluoro-uridine triphosphate
-
-
2'-C-ethynyl-4'-fluoro-uridine triphosphate
-
-
2'-C-ethynyl-uridine triphosphate
-
-
2'-C-methyl-3'-O-L-valylcytidine
-
-
2'-C-methyl-4'-fluoro-uridine triphosphate
-
-
2'-C-methyl-uridine triphosphate
-
-
2'-C-propynyl-4'-fluoro-uridine triphosphate
-
-
2'-C-propynyl-uridine triphosphate
-
-
2'-deoxy-2'-fluoro-2'-methylcytidine
-
-
2'-deoxy-2'-fluorocytidine
-
-
2'-deoxycytidine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-dGTP
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-fluoro-2'C-methylcytidine-5'-triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
2'-fluoro-2'C-methyluridine-5'-triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised. Although 2'C-modified CTP analogs are more efficiently incorporated compared with the UTP analog, the UTP analog is a better inhibitor because of its resistance to ATP-dependent excision
2'C-methylcytidine triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
2,3-bis(4-fluorophenyl)quinoxaline-6-carboxylic acid
-
2,3-bis(4-methylphenyl)quinoxaline-6-carboxylic acid
-
2,3-di-2-furylquinoxaline-6-carboxylic acid
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
2,3-diphenylquinoxaline-6-carboxylic acid
-
2,4-dioxo-4-phenylbutanoic acid
-
specific inhibitor
2-(2-C-methyl-b-D-ribofuranosyl)-2,6-dihydro-7H-2,3,5,6-tetraazabenzo[cd]azulen-7-one
-
-
2-(3-[[(2-chlorobenzyl)carbamoyl]amino]thiophen-2-yl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-(4-benzylphenyl)-3-cyclohexyl-1-methyl-1H-indole-6-carboxylic acid
-
-
2-(4-chlorophenyl)-3-cyclohexyl-1-[2-[4-(diethylamino)piperidin-1-yl]-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
2-(4-[[2-(4-acetylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[2-(4-carboxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[2-(4-chlorophenoxy)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[5-(acetylamino)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-([3-[1-(2-cyclopropylethyl)-6-fluoro-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
-
-
2-([3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
A-782759
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
-
-
2-([5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]-imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)-5-(pyrrolidin-1-ylsulfonyl)phenyl 1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxylate
-
-
2-amino-7-(2-C-methyl-beta-D-ribofuranosyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-bromo-5-methoxy-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
2-chloro-4-nitro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
2-cyano-N'-[(1Z)-(3,4,5-trihydroxyphenyl)methylene]acetohydrazide
-
-
2-fluoro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-5-(trifluoromethyl)benzamide
-
-
2-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-6-(trifluoromethyl)pyridine-3-carboxamide
-
-
2-nitro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)benzamide
-
-
2-[2-chloro-4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)phenyl]-2-methylpropanenitrile
-
-
2-[4-(2-[(2R)-2-cyclopentyl-4-hydroxy-5-[(6-methyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
-
-
2-[4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
-
-
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxamide
-
-
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-(benzyloxy)phenyl]-3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
2-[4-([4'-chloro-4-[(4-hydroxypiperidin-1-yl)carbonyl]biphenyl-2-yl]methoxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-([5-[acetyl(1-methylethyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-([5-[acetyl(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-[(5-chloro-2-morpholin-4-ylbenzyl)oxy]-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[5-[[4-(pyrrolidin-1-ylsulfonyl)phenyl]carbamoyl]-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzoic acid
-
-
3'-azido-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
3'-dATP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-dCTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-deoxy-5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)cytidine
-
-
3'-fluoro-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
3,4,5-trihydroxybenzaldehyde O-methyloxime
-
-
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
-
-
3-(2-C-methyl-b-D-ribofuranosyl)pyrido[2,3-d]pyrimidine-2,7(3H,8H)-dione
-
-
3-(3-nitrophenylazo)cytisine
3-(4-chlorophenylazo)cytisine
3-(benzyloxy)-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
3-(isopropyl[(4-methylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
3-([(2,4-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
3-([(4-chloro-2,5-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxamide
-
-
3-allyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-benzyl-5-chloropyrido[3,2-g]quinoxalin-2(1H)-one
-
moderate antiproliferative activity for the cell lines tested
3-butyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-cyclohexyl-1-(2-oxo-2-piperidin-1-ylethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-(2-[methyl[(1-methylpiperidin-3-yl)methyl]amino]-2-oxoethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-methyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-(4-methoxyphenyl)-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-(3-furyl)-1-methyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-(3-furyl)-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-furan-3-yl-1-[2-oxo-2-(4-pyrrolidin-1-ylpiperidin-1-yl)ethyl]-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1-methyl-1H-indole-6-carboxamide
-
-
3-cyclohexyl-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[3,2-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-3H-thieno[2,3-d]imidazole-5-carboxylic acid
-
-
3-cyclohexyl-2-phenylquinoline-6-carboxylic acid
-
-
3-oxo-3-[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]propanoic acid
-
-
3-tert-butyl-1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
3-[(4-amino-2-tert-butyl-5-methylphenyl)sulfanyl]-6-cyclopentyl-4-hydroxy-6-[2-(4-hydroxyphenyl)ethyl]-5,6-dihydro-2H-pyran-2-one
-
-
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenylthiophene-2-carboxylic acid
-
-
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylpiperidin-4-yl)amino]-5-phenylthiophene-2-carboxylic acid
-
-
3-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
4'-azido-cytidine triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
4'-azido-D-arabinofuranosylcytosine
-
-
4'-C-azidocytidine-5'-triphosphate
causes only partial chain termination
4-(2-C-methyl-b-D-ribofuranosyl)-3-oxo-3,4-dihydropyrazine-2-carboxamide
-
-
4-(chloromethyl)-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-amino-2-chloro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-bromo-1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
4-bromo-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
4-fluoro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
-
-
4-phenylazo-1-(phenyl)piperazine
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)-2'-O-methylcytidine
-
-
5,6-dihydroxy-2-(1,3-thiazol-5-yl)pyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-(2-thienyl)pyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-phenylpyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
-
-
5,8-dichloro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
5-((Z)-[(4-methylpiperazin-1-yl)imino]methyl)benzene-1,2,3-triol
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
5-(3-fluorobenzylidene)-2-[[5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(4-bromophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
reversible and non-competitive with nucleotides. Inhibitor appear to form a reversible covalent bond with the NS5B cysteine 366
5-(4-chlorophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
reversible and non-competitive with nucleotides. Inhibitor appear to form a reversible covalent bond with the NS5B cysteine 366
5-(4-cyanophenyl)-3-([(2-methylphenyl)sulfonyl]amino)thiophene-2-carboxylic acid
-
-
5-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
5-(4-[[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
5-(carboxymethoxy)-N-[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]-L-tryptophan
-
-
5-([3,5-bis(trifluoromethyl)phenyl]amino)-3-hydroxyisothiazole-4-carbonitrile
-
-
5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
-
i.e. DMB213. Competitive with natural nucleoside triphosphate substrates
5-chloro-3-phenylpyrido[3,2-g]quinoxalin-2(1H)-one
-
compound is equally cytotoxic for all cell lines tested
5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5-cyclopropyl-2-(4-fluorophenyl)-6-[(2-hydroxyethyl)(methylsulfonyl)amino]-N-methyl-1-benzofuran-3-carboxamide
-
-
5-ethyl-1-(2-C-methyl-b-D-ribofuranosyl)-1,5-dihydro-1,4,5,6,8-pentaazaacenaphthylen-3-amine
-
-
5-fluoro-7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
5-fluorouridine triphosphate
-
5-fluorouridine triphosphate is a strong competitive inhibitor of VPg uridylylation by FMDV 3D in vitro, versus UTP, FUTP, dTTP, ATP, CTP, or GTP, uridylylation at VPg Tyr3, which is located near the active site of 3D, at the RNA binding cleft of 3D, binding structure from crystal structure, overview. No inhibition with oligoT primers
5-hydroxy-N-[[3-(3-methoxyphenyl)-2-(4-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
5-phenyl-2H-1,2,3-triazole-4-carboxylic acid
-
5-[(3,5-dichlorophenyl)amino]-3-hydroxyisothiazole-4-carbonitrile
-
-
5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine
-
5-[(Z)-(morpholin-4-ylimino)methyl]benzene-1,2,3-triol
-
-
5-[(Z)-(phenylimino)methyl]benzene-1,2,3-triol
-
-
5-[[(4-chlorophenyl)sulfonyl]amino]-2-methyl-1-benzofuran-3-carboxylic acid
Q6DLV0
crystallization data, the inhibitor binds to the protein as a dimer and causes conformational changes in the protein
5BSL3.2N
-
the complementary strand of 5BSL3.2 inhibits the enzyme, the bulge structure is indispensable for enzyme binding
-
6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
6-cyclohexyl-4-methyl-5-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-cyclohexyl-4-[2-(dimethylamino)-2-oxoethyl]-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-cyclohexyl-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-ethoxy-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
6-furan-3-yl-9-b-D-ribofuranosyl-9H-purine
-
-
6-methoxy-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
6-[2-(3-chloro-4-methoxyphenyl)ethyl]-6-cyclopentyl-4-hydroxy-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-5,6-dihydro-2H-pyran-2-one
-
-
6-[2-(5-chloro-2,4-dimethoxyphenyl)ethyl]-6-cyclopentyl-3-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)sulfanyl]-4-hydroxy-5,6-dihydro-2H-pyran-2-one
-
AG-021541
6-[2-(methoxysulfinyl)hydrazino]-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
7-(2-C-methyl-b-D-ribofuranosyl)-5-nitro-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
8,8'-[carbonylbis(imino-3,1-phenylene carbonylimino)]bis(1,3,5-naphthalene-trisulfonic acid)
i.e. NF023
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
8-chloro-1-propyl-5-(trifluoromethyl)-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
8-cyano-5-fluoro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
8-cyano-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
8-cyano-7-fluoro-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
9-(5,6-dideoxy-2-C-methyl-6-phosphono-b-D-ribo-hexofuranosyl)-9H-purin-6-amine
-
-
9-(5,6-dideoxy-6-phosphono-b-D-ribo-hexofuranosyl)-9H-purin-6-amine
-
-
9-(5-O-[bis[2-(acetylsulfanyl)ethoxy]phosphoryl]-2-C-methyl-b-D-ribofuranosyl)-6-ethoxy-9H-purine
-
-
afzelin
strong binding affinity to the enzyme (RdRp)
alpha-Amanitin
-
alpha-amanitin inhibits extension of B2 RNA by Pol II in vitro
aptamer F38
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
aptamer F47
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
aptamer F52
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
Astragalin
strong binding affinity to the enzyme (RdRp)
azidothymidin triphosphate
-
benzyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]prolinate
-
-
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
beta-D-2'-beta-C-ethynyl-7-deaza-adenosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
beta-D-2'-beta-C-methyladenosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methylcytidine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methylguanosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyluridine-5'-triphosphate
beta-D-2'-deoxy-2'-alpha-fluoro-2'-beta-C-methylcytidine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-deoxy-2'-alpha-fluoro-2'-beta-C-methylguanosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
i.e. PSI-6130, a selective inhibitor of hepatitis C virus replication that targets the NS5B polymerase
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine 5'-triphosphate
-
PSI-6130-TP, potent inhibitor
beta-D-2'-deoxy-2'-fluoro-2'-C-methyluridine 5'-triphosphate
-
also named RO2433-TP or PSI-6206, potent inhibitor
biorobin
strong binding affinity to the enzyme (RdRp)
conivaptan
binds to RNA-dependent RNA polymerase with high affinity
cyclohexyl 4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)benzenesulfonate
-
-
cyclopropylindolobenzazepine inhibitors
-
cyclosporine A
inhibits HCV replication
ddGTP
-
IC50: above 0.2 mM
ddTTP
-
IC50 above 0.5 mM
delvomycin
-
the protein synthetic activity of the EF-Tu in the replicase complex is eliminated but the Qbeta RNA replicase activity is only slightly affected
dihydropyranone inhibitor
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
dimethyl (2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylate
-
-
eltrombopag
binds to RNA-dependent RNA polymerase with high affinity
ErbB3-binding protein 1
-
specifically interacts with the catalytic subunit PB1 of influenza virus RNA polymerase near the catalytic site for RNA polymerization
-
ergotamine
binds to RNA-dependent RNA polymerase with high affinity
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl (2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate
AG110, potent inhibitor of pestivirus replication, does not inhibit the in vitro activity of recombinant bovine viral diarrhea virus RdRp but inhibits the activity of bovine viral diarrhea virus replication complexes
Ethyl 4-(phenylazo)-piperazincarboxylate
fisetin
high affinities with the RNA-polymerase active site
Fructus Ligustri Lucidi aqueous extract
-
0.005 mg/ml, inhibits intracellular NS5B-catalyzed RNA synthesis
-
GDP
-
competitive with GTP
guanidine
-
blocks the initiation step of RNA synthesis in vitro
HA1077
-
i.e. fasudil, reduces the levels of intracellular viral RNA by 70% at 0.02 mM, the RdRp activity of HCV NS5B is not inhibited by the PRK2 inhibitor, but its activation by phosphorylation through PRK2
HgCl2
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol
IDX-184
high potential to fight the SARS-CoV-2 strain specifically
imidazole
tolerable at low concentrations, but inhibits at concentrations higher than 25 mM
indole diamide inhibitors
-
indole-N-acetamide inhibitors
-
indolo-benzoxazocine inhibitors
-
JTK-109
-
potent inhibitor
kaempferol
strong binding affinity to the enzyme (RdRp)
methyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboxylate
-
-
methyl 2-[5-[[4-(pyrrolidin-1-ylsulfonyl)phenyl]carbamoyl]-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzoate
-
-
methyl 5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl 6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
methyl N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(2-methoxy-2-oxoethoxy)-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(2-methoxy-2-oxoethoxy)-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
Myricitrin
strong binding affinity to the enzyme (RdRp)
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
N,1-dimethyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N,N'-[4-(pyrrolidin-1-ylsulfonyl)benzene-1,2-diyl]bis[1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide]
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboxamide
a non-nucleoside inhibitor
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboximidic acid
NIC02, in combination with NIC04, i.e. 1-benzyl-N-(2,3-dimethylphenyl)-3,5-dimethyl-1H-pyrazole-4-carboxamide
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-pent-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
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N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-prop-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
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N-(3-[4-hydroxy-5-[(E)-2-(4-methoxyphenyl)ethenyl]-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
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N-(3-[5-[(1E)-3,3-dimethylbut-1-en-1-yl]-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
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N-(4-[[2-(hydroxymethyl)piperidin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-(4-[[4-(methoxymethylidene)piperidin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-(4-[[4-(tert-butoxyamino)piperazin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-propyl-N-[2-(2H-1,2,4-triazino[5,6-b]indol-3-ylthio)ethyl]-1-propanamine
VP32947
N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepin-10-yl)carbonyl]-2-methylalanine
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N-[(1R)-6-chloro-2,3,4,9-tetrahydro-1H-carbazol-1-yl]pyridine-2-carboxamide
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N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
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N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
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N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
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N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
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N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(2,4-dichlorophenyl)carbonyl]-N-[3-(trifluoromethyl)benzyl]-L-phenylalanine
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N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
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N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
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N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
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N-[(5Z)-5-((5-[2-chloro-5-(trifluoromethyl)phenyl]-2-furyl)methylene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
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N-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
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N-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
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N-[(Z)-2-[4-(2-bromophenoxy)phenyl]-1-[(2-hydroxyethyl)carbamoyl]ethenyl]benzamide
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N-[2-amino-4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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N-[2-hydroxy-4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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N-[3-[(4aR,7aS)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,4a,5,6,7,7a-hexahydro-1H-cyclopenta[b]pyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(4R)-1-hydroxy-4-methyl-4-(3-methylbutyl)-3-oxo-3,4-dihydronaphthalen-2-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
A-837093
N-[3-[(4R)-5-(4-fluorobenzyl)-8-hydroxy-4-methyl-6-oxo-5-azaspiro[2.5]oct-7-en-7-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-5-propyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclobutyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclobutyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclohexyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclohexyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclohexyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-2-oxo-5-prop-2-yn-1-yl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopentyl-5-ethyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopropyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopropyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-1-cyclopropyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-5-butyl-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5R)-6-(4-fluorobenzyl)-9-hydroxy-5-methyl-7-oxo-6-azaspiro[3.5]non-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-1,5-bis(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-5-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-5-ethyl-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-5-tert-butyl-1-(3-chloro-4-fluorobenzyl)-4-hydroxy-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]-1,1-dioxido-4H-1,2-benzothiazin-7-yl]methanesulfonamide
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N-[3-[(5S)-5-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]-1,1-dioxido-1,2-benzisothiazol-6-yl]methanesulfonamide
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N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-6-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6R)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6R)-6-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6S)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6S)-1-(4-fluorobenzyl)-6-(4-fluorophenyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6S)-6-(1-ethylpropyl)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[(6S)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[1-(4-fluorobenzyl)-4-hydroxy-5,5-dimethyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
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N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-phenyl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-thiophen-2-yl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[5-acetyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[5-bromo-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[5-ethenyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[5-furan-2-yl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[6-(4-fluorobenzyl)-9-hydroxy-7-oxo-6-azaspiro[4.5]dec-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[3-[7-(4-fluorobenzyl)-10-hydroxy-8-oxo-7-azaspiro[4.5]dec-9-en-9-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
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N-[4-(1H-indol-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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N-[4-(1H-indol-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(azepan-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(azocan-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(cyclohexylsulfamoyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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N-[4-(diethylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(dimethylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(diprop-2-en-1-ylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(dipropylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1,3-benzothiazole-2-carboxamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-[2-(trifluoromethyl)phenyl]-1H-imidazole-2-carboxamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-2-(trifluoromethyl)benzamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)benzamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)benzamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]furan-2-carboxamide
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N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]thiophene-2-carboxamide
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N-[4-([4-[2-(2-hydroxyethoxy)ethyl]piperazin-1-yl]sulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[(2,6-dimethylpiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[(2-ethylpiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[(4-aminopiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[(4-hydroxypiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[(4-tert-butoxypiperazin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[bis(1-methylethyl)sulfamoyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[4-[bis(2-methylpropyl)sulfamoyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
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N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
N-[[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]methyl]-4-(pyrrolidin-1-ylsulfonyl)aniline
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N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
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N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(carboxymethoxy)-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(carboxymethoxy)-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
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N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
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N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
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N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
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N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
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N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
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N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
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N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
-
-
NEM
-
0.1 mM, reduces the transcription activity down to 10%
NTP
-
3Dpol is inhibited by NTP concentrations higher than 2 mM
p-Hydroxymercuriphenylsulfonate
-
0.1 mM, reduces the transcription activity down to 10%
pancreatic RNase
-
0.006 mg/ml, marked inhibition
-
PCMB
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol. PCMB-inhibited enzyme is unable to synthesize RNA, but still maintains template-binding ability
phenyl 1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]-L-prolinate
-
-
phenylalanine
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
Poly(U)
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
Polyethylene sulfonate
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-2-fluoro-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
the prodrug displays potent anti-dengue virus activity in the primary human peripheral blood mononuclear cell-based assay with no significant cytotoxicity in human hepatocellular liver carcinoma cell lines and no mitochondrial toxicity in the cell-based assay using human prostate cancer cell lines
quercetin
high affinities with the RNA-polymerase active site; strong binding affinity to the enzyme (RdRp)
quercetin-3'-O-glucuronide
better binding affinities than quercetin
quercetin-3'-O-sulfate
better binding affinities than quercetin
quercetin-3-O-glucoside
strong binding affinity to the enzyme (RdRp)
quercetin-3-O-glucuronide
better binding affinities than quercetin
quercetin-3-O-rutinoside
i.e. rutin, most active compared to all quercetin derivatives
quercetin-7-O-glucuronide
better binding affinities than quercetin
quercetin-7-O-sulfate
better binding affinities than quercetin
quercitrin
strong binding affinity to the enzyme (RdRp)
quinupristin
virtual screen identifies several drugs predicted to bind in the conserved RNA tunnel. Quinupristin is expected to bind across the RNA tunnel, blocking access from both sides and suggesting that it has the potential to arrest viral replication by preventing viral RNA synthesis. Quinupristin is an antibiotic that has been in clinical use for two decades and causes relatively minor side effects
R7128
is the prodrug of PSI-6130, inhibits the enzyme and viral replication
RNA
-
inhibited by high non-template RNA concentrations. This inhibition indicates feedback regulation of minus-strand synthesis
setrobuvir
high potential to fight the SARS-CoV-2 strain specifically
Sodium diphosphate
-
10 mM, decreases incorporation down to 5%
Tenofovir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
tert-butyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboperoxoate
-
-
tetracyclic indole inhibitors
-
thiophene
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
tipranavir
binds to RNA-dependent RNA polymerase with high affinity
Y27632
-
blocks HCV RdRp phosphorylation by suppressing PRK2 activation, reduces the levels of intracellular viral RNA by 92% at 0.02 mM, the RdRp activity of HCV NS5B is not inhibited by the PRK2 inhibitor, but its activation by phosphorylation through PRK2
YAK
high potential to fight the SARS-CoV-2 strain specifically
[(1R)-5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
[(1R)-8-chloro-5-ethyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
[(1S)-5-cyano-8-methyl-1-(1-methylpropyl)-7-[2-(1H-pyrazol-1-yl)ethoxy]-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]acetic acid
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
2'-C-ethynylcytidine
-
-
2'-C-methylcytidine
-
-
2'-C-methylguanosine
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
3'-dGTP
Q6DLV0
-
3'-dGTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-dUTP
-
incorporation of the 3'-deoxynucleotide triphosphate fully preventes extension of a product in the presence of the next correct ribonucleotide
3'-dUTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
4'-azidocytidine
-
-
4'-azidocytidine
-
R-1479, potent and highly selective inhibitor
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
in addition, inhibitory to the recombinant hepacivirus enzyme. Compound shows no cytotoxicity for the various cell lines tested, exception made for HepG-2 cells
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
in addition, inhibitory to the recombinant bovine viral diarrhea virus enzyme. Compound shows no cytotoxicity for the various cell lines tested, exception made for HepG-2 cells
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
6-azauridine
-
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
-
acycloguanosine
-
-
ATP
-
reaction at the U-incorporation site is inhibited with inhibition constant 1.09 mM, reaction at the G-incorporation site is inhibited with inhibition constant 1.25 mM, reaction at the C-incorporation site is inhibited with inhibition constant 1.48 mM
aurintricarboxylic acid
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
aurintricarboxylic acid
-
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
Ca2+
Cystovirus phi6
-
Ca2+
-
no activity at 3 mM
CTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 2.7 mM
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
favipiravir
-
favipiravir
unusually high nucleotide incorporation rates and high error rates of SARS-CoV RNA-dependent-RNA-polymerase allow facile insertion of Favipiravir into viral RNA, provoking C-to-U and G-to-A transitions in the already low cytosine content SARS-CoV-2 genome
galidesivir
-
galidesivir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
gliotoxin
-
-
gliotoxin
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
gliotoxin
-
IC50: 0.15 mM
GTP
-
competitive inhibitor of initiation but not of elongation
heparin
-
100 nM heparin rapidly inactivates 3Dpol by inhibiting reinitiation
heparin
-
0.0005 mM, 50% inhibition
KCl
-
reversible inhibition at high concentrations
KCl
-
50 mM, 90% inhibition
KCl
-
100 mM, slight decrease in activity
Mg2+
-
12.5 mM, replicase activity is reduced by 50%
Mn2+
-
above 2 mM
Mn2+
-
polymerase activity drops sharply at 3 mM
Mn2+
-
concentrations of 1.0 mM, 0.5 mM and 0.05 mM in the presence of Mg2+ inhibit activity by 75%, 50% and 25%, respectively
Mycophenolic acid
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
NaCl
-
at high concentrations
NaCl
-
150 mM or above, about 90% of acctivity is lost
NaCl
-
slight decrease in activity
NaCl
tolerable at low concentrations, but inhibits at concentrations higher than 25 mM
NADPH
-
the enzyme activity decreases when titrated with NADPH in vitro
NADPH
-
the inhibitor occupies the RNA template binding channel of Human enterovirus D68 enzyme (RdRp) with a binding pocket. Residues involved in the NADPH binding pocket of EV-D68 RdRp are highly conserved in RdRps of enteroviruses. The enzyme activity decreases when titrated with NADPH in vitro
polylysine
-
strong
polylysine
-
IC50: 250 ng/ml
ppGpp
-
competitive inhibitor of initiation but not of elongation
ppGpp
-
competitive with GTP
remdesivir
-
remdesivir
high-affinity and consistent molecular interactions with specific active site residues that anchor remdemsivir within the binding pocket for efficient binding. These residues are Asp452, Thr456, Arg555, Thr556, Val557, Arg624, Thr680, Ser681, and Ser682. Remdesivir binding induces minimal individual amino acid perturbations, subtly interferes with deviations of C-alpha atoms, and restricts the systematic transition of SARS-CoV-2 RNA-dependent RNA polymerase from the buried hydrophobic region to the surface-exposed hydrophilic region. A pharmacophore model based on the observed high-affinity interactions with SARSCoV-2 virus RNA-dependent RNA polymerase is mapped, which showcase the crucial functional moieties of remdesivir and is subsequently employed for virtual screening
remdesivir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
remdesivir
cryo-electron microscopy structure of the SARS-CoV-2 RNA-dependent RNA polymerase, both in the apo form at 2.8 A resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5 A resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RNA-dependent RNA polymerase, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation
remdesivir
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution. A comparative analysis model shows how remdesivir binds to this polymerase
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+3
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+5
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+3
remdesivir triphosphate
the structures of the enzyme in complex with RNA helical strands and remdesivir provide the structure details of RdRp inhibition by remdesivir. The inhibitor competes with the incorporation of nucleotide counterparts and inhibits transcription of viral RNA. The inhibition mechanism of remdesivir is a delayed chain termination of nascent viral RNA at i+3 position
remdesivir triphosphate
the inhibition mechanism of remdesivir triphosphate is inestigated through structural and kinetic analyses
remdesivir triphosphate
using pharmacophore models, three natural product hits SN00166900, SN00303170 and SN00359915 are identified which have lower binding energies than that of remdesivir triphosphate
remdesivir triphosphate
effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
remdesivir triphosphate
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+5
remdesivir triphosphate
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
ribavirin
-
-
ribavirin
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
RNase
-
pancreatic RNAse and T1 RNAse
-
RNase
-
RNAse A, 0.01 mg/ml, or Rnase T1, 0.002 mg/ml, inhibit the reaction by 90-95%
-
RNase
-
completely eliminates incorporation
-
sofosbuvir
-
-
sofosbuvir
-
the clinical effectiveness of sofosbuvir is largely a function of being intractable to nucleotide-mediated excision compared with similar nucleoside analogs
sofosbuvir
the enzyme (RdRp) of the SARS-CoV-2 RNA virus represents the most optimal target for an antiviral drug. Linear amino acid sequence as well as molecule structure show the highest homology to RdRps of other positive-sense RNA viruses. It is highly predictable that an antiviral developed for an RNA virus with a genome of the same polarity (i.e. sofosbuvir for HCV) could have a higher inhibitory efficacy against the SARS-CoV-2, compared to antiviral developed for negative-sense RNA viruses
sofosbuvir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
sofosbuvir triphosphate
-
-
sofosbuvir triphosphate
-
sofosbuvir triphosphate
sofosbuvir triphosphate is incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase. Sofosbuvir triphosphate is not incorporated by a host-like high-fidelity DNA polymerase
sofosbuvir triphosphate
-
-
spermine
-
-
spermine
-
1 mM, 50% inhibition
suramin
-
-
UTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 3.2 mM
Zn2+
-
complete inhibition at concentrations above 1.25 mM ZnCl2
Zn2+
-
IC50: 0.0006 mM, suppression of inhibition by dithiothreitol
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
the CSFC analogues 2-(2-furanyl)-N-(6-methyl-2-benzothiazolyl)-4-quinolinecarboxamide and 2-phenyl-N-(1-phenyl-1H-pyrazol-3-yl)-4-quinolinecarboxamide do not inhibit the in vitro activity of recombinant Bovine viral diarrhea virus RNA-dependent RNA polymerase but inhibit the activity of Bovine viral diarrhea virus replication complexes
-
additional information
-
activity is depressed by increasing monovalent ion concentrations
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
structure-based drug design of potent non-nucleoside inhibitors of Dengue viral RNA-dependent RNA polymerase, -ray-based fragment screening, overview. A biphenyl acetic acid fragment 3 binds in the palm subdomain of RdRp, 1000fold improvement in potency in vitro and acquired antidengue activity against all four serotypes with low micromolar EC50 in cell-based assays
-
additional information
-
activity is lowered at ionic strength of 0.1
-
additional information
-
inhibition of NS5B activity by RNA template exhibits characteristics of substrate inhibition, suggesting the template binds to a secondary site on the enzyme forming an inactive complex, poly(A) behaves like a competitive inhibitor with respect to oligo (dT12) primer
-
additional information
mAbs 8B2 and 7G8 inhibit the primer-dependent RdRp activity, mAb 8B2 inhibits the elongation of RNA chains, while mAb 7G8 inhibitory effect is achieved through inhibition of multiple RNA synthesis initiations
-
additional information
-
mAbs 8B2 and 7G8 inhibit the primer-dependent RdRp activity, mAb 8B2 inhibits the elongation of RNA chains, while mAb 7G8 inhibitory effect is achieved through inhibition of multiple RNA synthesis initiations
-
additional information
inhibitor efficiency with wild-type and mutant enzymes, overview
-
additional information
-
inhibitor efficiency with wild-type and mutant enzymes, overview
-
additional information
5,5- and 6,6-dialkyl-5,6-dihydro-1H-pyridin-2-ones as potent inhibitors of HCV NS5B polymerase, overview
-
additional information
-
5,5- and 6,6-dialkyl-5,6-dihydro-1H-pyridin-2-ones as potent inhibitors of HCV NS5B polymerase, overview
-
additional information
reduction of NS5B activity by co-expression of an NS5B mRNA-cleaving DNAzyme in Hep-G2 cells
-
additional information
-
reduction of NS5B activity by co-expression of an NS5B mRNA-cleaving DNAzyme in Hep-G2 cells
-
additional information
-
PRK2 inhibitors can be antiviral drugs that act by suppressing HCV replication via inhibition of viral RNA polymerase phosphorylation
-
additional information
-
not inhibitory: rifamycin
-
additional information
-
synthesis and evaluation of 4-thiazolidinones as non-nucleoside inhibitors of hepatitis C virus NS5B RNA-dependent RNA polymerase, docking study and molecular modelling, overview
-
additional information
-
non-nucleoside analogue inhibitors are being developed as part of a multidrug regiment to treat hepatitis C viral infections. Particularly promising are inhibitors that bind to the surface of the thumb domain of the viral RNA-dependent RNA polymerase. Kinetic analysis shows that non-nucleoside inhibitors binding to thumb site-2 (NNI2) do not block initiation or elongation of RNA synthesis, rather, they block the transition from the initiation to elongation, which is thought to proceed with significant structural rearrangement of the enzyme-RNA complex. Mapping of the effect of three NNI2 inhibitors on the conformational dynamics of the enzyme using hydrogen/deuterium exchange kinetics, overview. NNI2 inhibitors act through long range allosteric effects, revealing important conformational changes underlying normal polymerase function. Losses in conformational dynamics upon binding of NNI2s is correlated with inhibitor potency
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
inhibition of the assembly of the viral nucleoprotein, by RuvB-like protein 2, RBL2, and subsequent inhibition of the formation of the viral ribonucleoprotein complex inhibits viral RNA replication, overview
-
additional information
La France isometric virus
-
the enzyme is resistant to inhibitors of DNA-dependent RNA polymerase activity: actinomycin D, alpha-amanitin and rifampin
-
additional information
-
MNV-1 replication is insensitive to the fungal metabolite brefeldin A and consistently does not appear to recruit coatomer protein complex I, COPI, or COPII component proteins during replication
-
additional information
-
some pseudogene-derived siRNAs may be implicated in repressing pseudogene transcription involving RDR2
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
not sensitive to actinomycin D
-
additional information
-
the enzyme is resistant to 0.02 mg/ml rifampicin
-
additional information
MN908947
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
-
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution provides a basis for the design of new antiviral therapeutics that target viral RNA-dependent RNA polymerase
-
additional information
-
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution provides a basis for the design of new antiviral therapeutics that target viral RNA-dependent RNA polymerase
-
additional information
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
-
shRNAs expressing plasmids (pEGFP-U6/P1 and pEGFP-U6/P2) are capable of protecting cells against transmissible gastroenteritis virus invasion with very high specificity and efficiency against RdRp gene
-
additional information
-
the 5'-cap inhibits the (-)-strand RNA synthesis from the 3'-fold-back structure of (+)-strand RNA template without affecting the de novo synthesis of RNA
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
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0.000055
(2E)-3-(4-[[(1-[[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]amino]cyclobutyl)carbonyl]amino]phenyl)prop-2-enoic acid
Hepacivirus C
-
-
0.0013
(2E)-3-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)prop-2-enoic acid
Hepacivirus C
-
0.00069 - 0.0069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
0.0012
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0051
(2E)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0013
(2E)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.017
(2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0041
(2E)-3-[4-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0046
(2E)-3-[4-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.003
(2S)-(((5Z)-5-[(5-ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)amino)(4-fluorophenyl)acetic acid
Hepacivirus C
-
-
0.0031
(2S)-1-[(2-amino-4-chloro-5-methylphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.00008
(2S)-1-[(3,4,5-trichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.00077
(2S)-1-[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.0007
(2S)-2-[(2,4-dichlorobenzoyl)(3-nitrobenzyl)amino]-3-phenylpropanoic acid
Hepacivirus C
-
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
0.0011
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-thiophen-2-ylpyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.00019 - 0.02
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
0.02
(2S,4S,5R)-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
full-length enzyme
0.0067
(2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
Hepacivirus C
-
-
0.0001
(2Z)-2-(benzoylamino)-3-[4-(2-bromophenoxy)phenyl]acrylic acid
Hepacivirus C
-
-
0.0051
(2Z)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0013
(2Z)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0032
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.001
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000014
(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00002
(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00043
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00073
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00044
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000005
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000019
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0031
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00423
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-[[(2-phenylethoxy)sulfinyl]carbamoyl]-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.022
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00097 - 0.0044
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
0.068
(4S,5R)-4-(benzylcarbamoyl)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00315
(4S,5R)-4-[[(benzyloxy)sulfinyl]carbamoyl]-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.03
(5,7-difluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.0023
(5,8-dicyano-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.000055
(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
Hepacivirus C
-
-
0.0021
(5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.00057
(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
Hepacivirus C
-
-
0.0021
(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.0023
(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0004
1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.00001
1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
-
0.00011 - 0.00028
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
0.001
1-cyclohexyl-2-(2-fluoro-4-[[2-(3-oxomorpholin-4-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00015
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-hydroxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00013
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-methylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00041
1-cyclohexyl-2-(2-fluoro-4-[[2-methoxy-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00009
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopiperidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000066
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00015
1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0016
1-cyclohexyl-2-(3-furyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00003
1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
Hepacivirus C
-
-
0.00064
1-cyclohexyl-2-(4-[[4-(dimethylcarbamoyl)phenyl](phenyl)methoxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000071
1-cyclohexyl-2-(4-[[5-(1,1-dioxidoisothiazolidin-2-yl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000068
1-cyclohexyl-2-(4-[[5-(dimethylcarbamoyl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0003
1-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1H-benzimidazole-5-carboxamide
Hepacivirus C
-
-
0.0065
1-cyclohexyl-2-phenyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0004
1-cyclohexyl-2-phenyl-1H-indole-5-carboxylic acid
Hepacivirus C
-
-
0.000048
1-cyclohexyl-2-[2-fluoro-4-([5-[(1-methylethyl)carbamoyl]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000099
1-cyclohexyl-2-[2-fluoro-4-([5-[(methoxyacetyl)(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00013
1-cyclohexyl-2-[2-fluoro-4-[(2-morpholin-4-ylbenzyl)oxy]phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00014
12-cyclohexylindolo[1,2-c][1,3]benzoxazine-9-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 24°
0.0000072
13-cyclohexyl-3-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.000009
13-cyclohexyl-5-(2-piperidin-1-ylethyl)-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
Hepacivirus C
-
-
0.000021
13-cyclohexyl-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 46°
0.000077
13-cyclohexyl-6,7-dihydro-5H-indolo[2,1-a][2]benzazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 53°
0.000038
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzothiazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 56°
0.000026
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 43°
0.000047
14-cyclohexyl-7,8-dihydro-6H-indolo[1,2-e][1,5]benzoxazocine-11-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 61°
0.0159
2'-C-ethynyl-2'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00065
2'-C-ethynyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0016
2'-C-ethynyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0066
2'-C-methyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.005
2'-C-methyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0019
2'-C-methyladenosine
Hepacivirus C
-
-
0.00009 - 0.01
2'-C-methylcytidine
0.00013
2'-C-methylguanosine
Hepacivirus C
-
-
0.0028
2'-C-propynyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.002
2'-C-propynyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0038
2'-O-methylcytidine
Hepacivirus C
-
-
0.0055
2,3-bis(4-fluorophenyl)quinoxaline-6-carboxylic acid
Hepacivirus C
-
0.04
2,3-bis(4-methylphenyl)quinoxaline-6-carboxylic acid
Hepacivirus C
-
0.017
2,3-di-2-furylquinoxaline-6-carboxylic acid
Hepacivirus C
-
0.079
2,3-diphenylquinoxaline-6-carboxylic acid
Hepacivirus C
-
0.004
2,4-dioxo-4-phenylbutanoic acid
Hepacivirus C
-
30°C, pH 8.0
0.0015
2-(3-[[(2-chlorobenzyl)carbamoyl]amino]thiophen-2-yl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.00012
2-(4-benzylphenyl)-3-cyclohexyl-1-methyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000009
2-(4-chlorophenyl)-3-cyclohexyl-1-[2-[4-(diethylamino)piperidin-1-yl]-2-oxoethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00011
2-(4-[[2-(4-acetylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00018
2-(4-[[2-(4-carboxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00023
2-(4-[[2-(4-chlorophenoxy)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000017
2-(4-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00007
2-(4-[[5-(acetylamino)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000018
2-([3-[1-(2-cyclopropylethyl)-6-fluoro-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
-
0.000016 - 0.000046
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
0.0001
2-amino-7-(2-C-methyl-beta-D-ribofuranosyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Hepacivirus C
-
-
0.007
2-cyano-N'-[(1Z)-(3,4,5-trihydroxyphenyl)methylene]acetohydrazide
Hepacivirus C
-
-
0.000036
2-[2-chloro-4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)phenyl]-2-methylpropanenitrile
Hepacivirus C
-
wild type enzyme
0.000004
2-[4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
Hepacivirus C
-
wild type enzyme
0.0032
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000006
2-[4-(benzyloxy)phenyl]-3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000014
2-[4-([4'-chloro-4-[(4-hydroxypiperidin-1-yl)carbonyl]biphenyl-2-yl]methoxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000042
2-[4-([5-[acetyl(1-methylethyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000051
2-[4-([5-[acetyl(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0001
2-[4-[(5-chloro-2-morpholin-4-ylbenzyl)oxy]-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0012
3'-deoxycytidine
Hepacivirus C
-
-
0.00022
3'-dGTP
Dengue virus
Q6DLV0
-
0.00067 - 0.00068
3'-dUTP
0.012
3,4,5-trihydroxybenzaldehyde O-methyloxime
Hepacivirus C
-
-
0.000032
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
Hepacivirus C
-
-
0.000017
3-(benzyloxy)-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.008
3-(isopropyl[(4-methylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.0014
3-([(2,4-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.012
3-([(4-chloro-2,5-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxamide
Hepacivirus C
-
-
0.0012
3-allyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0145
3-allyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.011
3-allyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0063
3-allyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0012
3-benzyl-5-chloropyrido[3,2-g]quinoxalin-2(1H)-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.0019
3-butyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0054
3-butyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0046
3-butyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0015
3-butyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.00003
3-cyclohexyl-1-(2-oxo-2-piperidin-1-ylethyl)-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000018
3-cyclohexyl-1-(2-[methyl[(1-methylpiperidin-3-yl)methyl]amino]-2-oxoethyl)-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.0000072
3-cyclohexyl-1-methyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000018
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-(4-methoxyphenyl)-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00006
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00032
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
Hepacivirus C
-
-
0.000016
3-cyclohexyl-2-(3-furyl)-1-methyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00003
3-cyclohexyl-2-(3-furyl)-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000015
3-cyclohexyl-2-furan-3-yl-1-[2-oxo-2-(4-pyrrolidin-1-ylpiperidin-1-yl)ethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.0001
3-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1-methyl-1H-indole-6-carboxamide
Hepacivirus C
-
-
0.000046
3-cyclohexyl-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00015
3-cyclohexyl-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
Hepacivirus C
-
-
0.0019
3-cyclohexyl-2-phenyl-1H-pyrrolo[3,2-b]pyridine-6-carboxylic acid
Hepacivirus C
-
-
0.0138
3-cyclohexyl-2-phenyl-3H-thieno[2,3-d]imidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0048
3-cyclohexyl-2-phenylquinoline-6-carboxylic acid
Hepacivirus C
-
-
0.003
3-oxo-3-[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]propanoic acid
Hepacivirus C
-
-
0.00093
3-[(4-amino-2-tert-butyl-5-methylphenyl)sulfanyl]-6-cyclopentyl-4-hydroxy-6-[2-(4-hydroxyphenyl)ethyl]-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
-
0.0015
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.000019
3-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.00006 - 0.0008
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
0.0021
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
Hepacivirus C
-
-
1
5'-formylpyrogallol
Hepacivirus C
-
-
0.00076
5,6-dihydroxy-2-(1,3-thiazol-5-yl)pyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.0026
5,6-dihydroxy-2-(2-thienyl)pyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.03
5,6-dihydroxy-2-phenylpyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.00003
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.0032
5,8-dichloro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.00055 - 0.0021
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
0.005
5-((Z)-[(4-methylpiperazin-1-yl)imino]methyl)benzene-1,2,3-triol
Hepacivirus C
-
-
0.0032
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.00044
5-(4-bromophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
Hepacivirus C
-
37°C, pH 7.5
0.00054
5-(4-chlorophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
Hepacivirus C
-
37°C, pH 7.5
0.00027
5-(4-cyanophenyl)-3-([(2-methylphenyl)sulfonyl]amino)thiophene-2-carboxylic acid
Hepacivirus C
-
-
0.0018
5-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
Hepacivirus C
-
0.0016
5-(4-[[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
Hepacivirus C
-
0.000027
5-(carboxymethoxy)-N-[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
-
0.0059
5-([3,5-bis(trifluoromethyl)phenyl]amino)-3-hydroxyisothiazole-4-carbonitrile
Hepacivirus C
-
-
0.0052
5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
Zika virus
-
30°C, pH 6.8
0.001
5-chloro-3-phenylpyrido[3,2-g]quinoxalin-2(1H)-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.01
5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.015
5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.015
5-hydroxy-N-[[3-(3-methoxyphenyl)-2-(4-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0002
5-[(3,5-dichlorophenyl)amino]-3-hydroxyisothiazole-4-carbonitrile
Hepacivirus C
-
-
0.01
5-[(Z)-(morpholin-4-ylimino)methyl]benzene-1,2,3-triol
Hepacivirus C
-
-
0.5
5-[(Z)-(phenylimino)methyl]benzene-1,2,3-triol
Hepacivirus C
-
-
0.0032
6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.00001
6-cyclohexyl-4-methyl-5-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
Hepacivirus C
-
-
0.00006
6-cyclohexyl-4-[2-(dimethylamino)-2-oxoethyl]-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
Hepacivirus C
-
-
0.00007
6-cyclohexyl-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
Hepacivirus C
-
-
0.000038
6-[2-(3-chloro-4-methoxyphenyl)ethyl]-6-cyclopentyl-4-hydroxy-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
-
0.00002
6-[2-(5-chloro-2,4-dimethoxyphenyl)ethyl]-6-cyclopentyl-3-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)sulfanyl]-4-hydroxy-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
wild type enzyme
0.00012
7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Hepacivirus C
-
-
0.0002
8,8'-[carbonylbis(imino-3,1-phenylene carbonylimino)]bis(1,3,5-naphthalene-trisulfonic acid)
Murine norovirus 1
pH and temperature not specified in the publication
0.0000715 - 0.00028
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
0.0058
8-chloro-1-propyl-5-(trifluoromethyl)-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.0081
8-cyano-5-fluoro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0047
8-cyano-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0018
8-cyano-7-fluoro-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0000003 - 0.0000007
A-837093
0.0000158
aptamer F38
Foot-and-mouth disease virus
-
-
-
0.0000106
aptamer F47
Foot-and-mouth disease virus
-
-
-
0.0000164
aptamer F52
Foot-and-mouth disease virus
-
-
-
0.0053
ATP
rhinovirus A16
-
IC50: 0.0053 mM
0.05513 - 0.09076
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
0.00033 - 0.00046
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
0.00494 - 0.00578
beta-D-2'-beta-C-methyluridine-5'-triphosphate
0.00011 - 0.0007
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
0.0015
CTP
rhinovirus A16
-
IC50: 0.0015 mM
0.5
dATP
rhinovirus A16
-
IC50 above 0.5 mM
0.04
dCTP
rhinovirus A16
-
IC50: 0.04 mM
1
ddATP
rhinovirus A16
-
IC50 above 1 mM
1
ddCTP
rhinovirus A16
-
IC50 above 1 mM
0.2
ddGTP
rhinovirus A16
-
IC50: above 0.2 mM
0.5
ddTTP
rhinovirus A16
-
IC50 above 0.5 mM
0.1
dGTP
rhinovirus A16
-
IC50: 0.1 mM
0.5
dTTP
rhinovirus A16
-
IC50 above 0.5 mM
0.037
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
-
0.1
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
IC50 above 0.1 mM
0.1
ethyl (2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
IC50 above 0.1 mM
0.0002
GTP
rhinovirus A16
-
IC50: 0.0002 mM
0.000017
JTK-109
Hepacivirus C
-
-
0.0086
methyl 5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
-
0.0086
methyl 6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
-
0.026
methyl N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.072
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.072
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.026
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(2-methoxy-2-oxoethoxy)-L-tryptophanate
Hepacivirus C
-
0.0055
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.053
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(2-methoxy-2-oxoethoxy)-L-tryptophanate
Hepacivirus C
-
0.0055
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.053
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.049
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.049
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.0199
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboxamide
Rabbit hemorrhagic disease virus
pH 7.5, 30°C, recombinant enzyme
0.000067
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-pent-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000006
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-prop-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.00048
N-(3-[4-hydroxy-5-[(E)-2-(4-methoxyphenyl)ethenyl]-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000406
N-(3-[5-[(1E)-3,3-dimethylbut-1-en-1-yl]-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000046
N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepin-10-yl)carbonyl]-2-methylalanine
Hepacivirus C
-
-
0.016
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.033
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.01
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.011
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.015
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.1
N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
IC50 above 0.1 mM
0.016
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.033
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0017
N-[(2,4-dichlorophenyl)carbonyl]-N-[3-(trifluoromethyl)benzyl]-L-phenylalanine
Hepacivirus C
-
-
0.005
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0037
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0006
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0018
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0002
N-[(5Z)-5-((5-[2-chloro-5-(trifluoromethyl)phenyl]-2-furyl)methylene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.00028
N-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.00044
N-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.0027
N-[(Z)-2-[4-(2-bromophenoxy)phenyl]-1-[(2-hydroxyethyl)carbamoyl]ethenyl]benzamide
Hepacivirus C
-
-
0.000025
N-[3-[(4aR,7aS)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,4a,5,6,7,7a-hexahydro-1H-cyclopenta[b]pyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.000037
N-[3-[(4R)-5-(4-fluorobenzyl)-8-hydroxy-4-methyl-6-oxo-5-azaspiro[2.5]oct-7-en-7-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00011
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-5-propyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000044
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000025
N-[3-[(5R)-1-cyclobutyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.00017
N-[3-[(5R)-1-cyclobutyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00017
N-[3-[(5R)-1-cyclohexyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00065
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00012
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000061
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000057
N-[3-[(5R)-1-cyclopentyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000048
N-[3-[(5R)-1-cyclopentyl-5-ethyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000068
N-[3-[(5R)-1-cyclopropyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000075
N-[3-[(5R)-1-cyclopropyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000049
N-[3-[(5R)-5-butyl-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00012
N-[3-[(5R)-6-(4-fluorobenzyl)-9-hydroxy-5-methyl-7-oxo-6-azaspiro[3.5]non-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.0014
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000045
N-[3-[(5S)-5-ethyl-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00017
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-6-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000026
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000042
N-[3-[(6R)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000042
N-[3-[(6R)-6-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.0001
N-[3-[(6S)-1-(4-fluorobenzyl)-6-(4-fluorophenyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000061
N-[3-[(6S)-6-(1-ethylpropyl)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000025
N-[3-[(6S)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.00018
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000085
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-5,5-dimethyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000004 - 0.000005
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
0.000002 - 0.000006
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
0.000274
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000425
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-phenyl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000011
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-thiophen-2-yl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.00028
N-[3-[5-acetyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000055
N-[3-[5-bromo-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000024
N-[3-[5-ethenyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000008
N-[3-[5-furan-2-yl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.00015
N-[3-[6-(4-fluorobenzyl)-9-hydroxy-7-oxo-6-azaspiro[4.5]dec-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00022
N-[3-[7-(4-fluorobenzyl)-10-hydroxy-8-oxo-7-azaspiro[4.5]dec-9-en-9-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.015
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.1
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
IC50 above 0.1 mM
0.0017
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(carboxymethoxy)-L-tryptophan
Hepacivirus C
-
0.0013
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0022
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
Hepacivirus C
-
0.0017
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(carboxymethoxy)-L-tryptophan
Hepacivirus C
-
0.0013
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.0022
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
Hepacivirus C
-
0.0019
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0061
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0061
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.0041
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0034
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0046
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0016
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.000034 - 0.00047
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
0.0019
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00019
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00045
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.009
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0011
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00057
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-2-fluoro-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.01
pyrogallol
Hepacivirus C
-
-
0.00026 - 0.00214
remdesivir triphosphate
0.0012
sofosbuvir
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0073 - 0.018
sofosbuvir triphosphate
0.0000246 - 0.0002
suramin
0.0023
UTP
rhinovirus A16
-
IC50: 0.0023 mM
0.0006
Zn2+
rhinovirus A16
-
IC50: 0.0006 mM, suppression of inhibition by dithiothreitol
0.00033
[(1R)-5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.003
[(1R)-8-chloro-5-ethyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.000002
[(1S)-5-cyano-8-methyl-1-(1-methylpropyl)-7-[2-(1H-pyrazol-1-yl)ethoxy]-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.09
[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]acetic acid
Hepacivirus C
-
-
0.00069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
full-length enzyme
0.00019
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.02
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.00097
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0044
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00011
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
polymerase from 1 b genotype
0.00028
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
polymerase from 1 a genotype
0.00009
2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1a
0.00018
2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1b
0.0012
2'-C-methylcytidine
Hepacivirus C
-
-
0.01
2'-C-methylcytidine
Hepacivirus C
mutant S282T
0.000016
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000046
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
polymerase from 1 a genotype
0.00067
3'-dUTP
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00068
3'-dUTP
Dengue virus
-
pH 7.5, 35°C
0.00006
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.0008
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
Hepacivirus C
-
pH 7.0, 22°C
0.00055
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0021
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0000715
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
norovirus
-
wild-type, pH 7.5, 30°C
0.00028
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
norovirus
-
mutant Y41A, pH 7.5, 30°C
0.0000003
A-837093
Hepacivirus C
-
polymerase from 1 b genotype
0.0000007
A-837093
Hepacivirus C
-
polymerase from 1 b genotype
0.05513
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
Dengue virus
-
pH 7.5, 35°C
0.09076
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00033
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
Dengue virus
-
pH 7.5, 35°C
0.00046
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00494
beta-D-2'-beta-C-methyluridine-5'-triphosphate
Dengue virus
-
pH 7.5, 35°C
0.00578
beta-D-2'-beta-C-methyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00011
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1b
0.00013
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1a
0.0007
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
Hepacivirus C
mutant S282T
0.15
gliotoxin
rhinovirus A16
-
IC50: 0.15 mM
0.202
gliotoxin
Hepacivirus C
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
0.000004
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000005
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
Hepacivirus C
-
polymerase from 1 a genotype
0.000002
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000002
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
polymerase from 1 a genotype
0.000006
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000034
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
Hepacivirus C
-
polymerase from 1 b genotype
0.00047
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
Hepacivirus C
-
polymerase from 1 a genotype
0.00026
remdesivir triphosphate
Yellow fever virus
-
pH and temperature not specified in the publication
0.00101
remdesivir triphosphate
Tick-borne encephalitis virus
pH and temperature not specified in the publication
0.00136
remdesivir triphosphate
Zika virus
pH and temperature not specified in the publication
0.0014
remdesivir triphosphate
Dengue virus type 3
-
pH and temperature not specified in the publication
0.00166
remdesivir triphosphate
West Nile virus
-
pH and temperature not specified in the publication
0.00214
remdesivir triphosphate
Japanese encephalitis virus
-
pH and temperature not specified in the publication
0.0073
sofosbuvir triphosphate
Zika virus
-
30°C, pH 6.8
0.018
sofosbuvir triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0000246
suramin
norovirus
-
wild-type, pH 7.5, 30°C
0.00007
suramin
Murine norovirus
-
wild-type, pH 7.5, 30°C
0.00007
suramin
Murine norovirus 1
pH and temperature not specified in the publication
0.00014
suramin
norovirus
-
mutant Y41A, pH 7.5, 30°C
0.0002
suramin
Murine norovirus
-
mutant Y41A, pH 7.5, 30°C
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D682A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
D683A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
C768Y
Q9LKP0
a C-to-T missense mutation in the first exon, the naturally occuring mutant rdr6-11 of RDR6 shows simultaneously enhanced SI and stigma exsertion, without associated increases in SRK transcript levels, phenotype, overview. The mutant exhibits stochastic stigma exsertion, and the S-locus receptor kinase, SRK, gene further enhances pistil elongation and stigma exsertion in this mutant background, a process that requires SRK catalytic activity and correlates with SRK transcript levels. rdr6-11 mutant plants are fertile and produce full siliques. By contrast, self-pollination of rdr6-11::Sb stigmas results in very low numbers of seeds per silique, indicating that mutant stigmas maintain SI into late stages of flower development even upon prolonged pollen-stigma contact
E291G
mutant is insensitive against inhibitor ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate
F224P
-
2-phenyl-N-(1-phenyl-1H-pyrazol-3-yl)-4-quinolinecarboxamide (CSFCII) resistant bovine viral diarrhea virus variants carry the F224P mutation in the viral RNA-dependent RNA polymerase (RdRp)
F224S
mutant is insensitive against inhibitors ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate, 5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine, and VP32947
F224Y/N264D
-
2-(2-furanyl)-N-(6-methyl-2-benzothiazolyl)-4-quinolinecarboxamide (CSFCI) resistant bovine viral diarrhea virus variants carry two mutations in the viral RNA-dependent RNA polymerase (RdRp), N264D and F224Y
F364A
-
the hydrophobic mutation leads to conformations with closed active site
F364W
-
the mutant enzym has no preference between the open and closed active sites, similar to wild-type enzyme
F364Y
-
mutation results in structure with open active site
E1069A
-
the mutation in RNA-dependent RNA polymerase can prevent the superinfection of the virus, with protection efficiency of 100%
E139Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E165A
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E165Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E168Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E172Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
E634Q
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket, the mutation to glutamine E634 eliminates this salt bridge without major disruption of the internal packaging within the polymerase
E652Q
Cystovirus phi6
-
site-directed mutagenesis in the plough region
K147L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
K451A
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
K451L
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
K541A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
K541L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
K627A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
K627L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
L628S
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R146L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel
R291K
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R291S
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
R30A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
T633A
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket
D238E
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.04% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.74% of the activity of the wild-type enzyme
D238F
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 4.4% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D238N
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.05% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.797% of the activity of the wild-type enzyme
D238V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 11% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D328A/D329A
-
site-directed mutagenesis
D339A/S341A/D349A
-
site-directed mutagenesis, the mutant shows a partial loss of oligomerization with the less severe viral phenotype
G1A
-
mutant is only partially active and the N-terminal hydrogen-bonding network is partly disrupted
IF-KH I331F/K359H
-
the mutant is competent for copy-choice recombination
IF-PS-KH I331F/P356S/K359H
-
the triple mutant replicates even faster but still exhibits a significant reduction in the rate of replication relative to wild-type enzyme. The virus is impaired substantially for recombination in cells
K359H
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type. K359H poliovirus is genetically unstable and acquires mutations encoding two second-site amino acid substitutions after a few passages in cell cultures
K359R
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type
L446D
-
mutant with disrupt interface I of 3Dpol
L446N/R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
L446N/R455A/R456A/D328A/D329A
-
site-directed mutagenesis, catalytically complete inactive mutant
N297D
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 89% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 38.2% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 21.2% of the activity of the wild-type enzyme
N297Q
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 35% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 1.4% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.72% of the activity of the wild-type enzyme
N297V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 55% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 15.3% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 4.9% of the activity of the wild-type enzyme
PS-KH P356S/K359H
-
the mutant is competent for forced-copy-choice recombination
R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
R455D
-
mutant with disrupt interface I of 3Dpol
V33A/F34A
-
site-directed mutagenesis
V391L
-
naturally occuring mutant, temperature-sensitive mutant. Some function of V391L polymerase other than its catalytic activity can be supplemented at the nonpermissive temperature, most likely via the formation of oligomeric structures on the surface of membranous vesicles that facilitate the tethering of the active enzyme
M296I
-
the mutant exhibits reduced sensitivity to ribavirin
K802A
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802G
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802N
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802P
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802Q
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
A105S
62% activity compared to the wild type enzyme
A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
A97S
88% activity compared to the wild type enzyme
C274A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
D225A
-
mutant enzyme is capable of robust de novo initiation in the presence of Mn2+, produces reduced amounts of product of 38 nt and longer that arose from template switch
D559G
mutant with decreased susceptibility for inhibitor A-837093
E18A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
F101A
89% activity compared to the wild type enzyme
F101Y
134% activity compared to the wild type enzyme
G102A
32% activity compared to the wild type enzyme
G104A
146% activity compared to the wild type enzyme
G554D
mutant with decreased susceptibility for inhibitor A-837093
H502A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
H95S
104% activity compared to the wild type enzyme
I11V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I11V/I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I239L
the mutation occurs under PSI-6130 selection in cell culture, it increases the enzyme activity compared to the wild-type enzyme
I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
I432V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I482S
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
I482T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
K100I
20% activity compared to the wild type enzyme
K72M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T/L564M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81S/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
M423I
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423V
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M426T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
P495A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P496A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P538T
naturally occuring mutation, location in the protein and role in RNA binding, overview
P540A
naturally occuring mutation, lethal effect of P540A mutation
P93A
90% activity compared to the wild type enzyme
P94A
115% activity compared to the wild type enzyme
Q438R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Q438R/E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
R158A
-
mutation decreases de novo initiation of RNA synthesis
R158A/R367A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R394A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R32A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32K
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32S
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R386A
-
mutation decreases de novo initiation of RNA synthesis
R394A
-
mutation decreases de novo initiation of RNA synthesis
R48A
-
mutation decreases de novo initiation of RNA synthesis
R503A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
R556V
naturally occuring mutation, location in the protein and role in RNA binding, overview
R98I
68% activity compared to the wild type enzyme
R98K
157% activity compared to the wild type enzyme
S282S/T/C575S/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G/V485L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/K81R/S84S/P I239L/A300T/L320F/L/C, A421V, Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S29A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
S368A
mutant with decreased susceptibility for inhibitor A-837093
S556G
naturally occuring mutation, location in the protein and role in RNA binding, overview
S96T
82% activity compared to the wild type enzyme
S96T/N142T
the mutation of the NS5B polymerase mediates resistance to R7128. Long-term culture selection with PSI-6130 in replicon cells harboring preexisting mutation S96T/N142T results in the emergence of the S282T substitution and the reversion of S96T to wild-type serine
T92S
18% activity compared to the wild type enzyme
V405L
naturally occuring mutation, location in the protein and role in RNA binding, overview
V494A
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
V499A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation increases RNA replication in cells
V499G
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
W550R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Y103F
89% activity compared to the wild type enzyme
Y191A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
Y276A
-
mutation completely abolishes RNA-dependent RNA polymerase activity
Y448H
mutant with decreased susceptibility for inhibitor A-837093
Y555C
mutant with decreased susceptibility for inhibitor A-837093
Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L640D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
D541A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
R734A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
R742A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S604A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
S604A-D541A
site-directed mutagenesis, the mutant shows no detectable primer extension activity
S799A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S799Y
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
D541A
-
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
-
R734A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
R742A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799Y
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
W460A
-
activity comparable to wild-type
W460F
-
activity comparable to wild-type
W460Y
-
activity comparable to wild-type
Y41A
-
mutation in inhibitor-binding site, about 5fold increase in IC50 values for inhibitors suramin and 8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
N812A
active site variant of RSV L-protein in the RSV L/P complex. The RSV L(N812A)/P complex does not produce RNA products with TrC sequence RNA as template
A185V
mutation causes change in secondary structure
A466V
mutation has no effect on secondary structure
A97V
mutation causes change in secondary structure
I201L
mutation has no effect on secondary structure
L329I
mutation has no effect on secondary structure
P323L
mutation causes change in secondary structure
V880I
mutation has no effect on secondary structure
A365N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
T363N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
T537I
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
A365N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
-
T363N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
T537I
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
S604T
-
the mutation confers resistance to nucleotide inhibitors, also conferred resistance to sofosbuvir triphosphate but not to 5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
D238A
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.24% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 1.9% of the activity of the wild-type enzyme
D238A
-
mutation destabilizes the catalytically competent enzyme-primer/template-NTP complex and reduces the efficiency of phosphoryl transfer
G64S
-
inactive
G64S
-
mutation of the key structural element of the alpha-helix in poliovirus RdRP, leads to the appearance of virus that reproduced better than the wild-type, the mutation stabilizes the interaction f Gly64 with residues Ala239 and Leu241 of the fingers subdomain
N297A
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 89% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 11.2% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 4.5% of the activity of the wild-type enzyme
N297A
-
mutation destabilizes the catalytically competent enzyme-primer/template-NTP complex and reduces the efficiency of phosphoryl transfer
S282T
-
the mutation shows reduced sensitivity to 2'-hydroxy-2'-C-methyl nucleosides
S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme. The mutation of the NS5B polymerase mediates a three to sixfold loss of sensitivity to PSI-6130 compared to the wild-type enzyme, lack of cross-resistance between PSI-6130 and R1479, overview
D536A
-
inactive
D536A
-
completely inactive enzyme
D668A
-
inactive
D668A
-
completely inactive enzyme
D669A
-
inactive
D669A
-
completely inactive enzyme
D669N
-
reduction in activity to about 5% relative to the parental NS5
D669N
-
mutant shows a reduction in activity to about 5% relative to the wild type enzyme
G605A
-
inactive
G605A
-
completely inactive enzyme
K691A
-
inactive
K691A
-
completely inactive enzyme
D536A
-
inactive
-
D536A
-
completely inactive enzyme
-
K691A
-
inactive
-
K691A
-
completely inactive enzyme
-
additional information
-
construction of dr2 knockout mutant plants, rdr2-1, showing reduced asymmetric 5S rDNA methylation at chromosomes 4 and 5 compared to the wild-type enzyme
additional information
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construction of rdr1 and rdr6 mutants, that exhibit globally reduced levels of viral small RNA production as well as reduced strand bias in viral small RNA population, revealing an important role for these host RDRs in viral siRNA biogenesis, analysis of Tobacco Mosaic Virus small RNA profile in Arabidopsis thaliana wild-type plants as well as rdr mutants rdr1-1 and rdr6-15 by applying small RNA deep sequencing technology, overview
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RNA-dependent RNA polymerase activity remains in truncated proteins coding for the amino acids from position 514 or 893 to the C terminus
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identification of RRF-3 siRNAs, overview. RRF-3 suppression by siRNA results in pleiotropic effects in sperm development, the sperm defects lead to embryonic lethality, nuclei of the mutant sperms are surrounded by ectopic microtubule structures with spindle abnormalities, phenotype, overview
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identification of RRF-3 siRNAs, overview. RRF-3 suppression by siRNA results in pleiotropic effects in sperm development, the sperm defects lead to embryonic lethality, nuclei of the mutant sperms are surrounded by ectopic microtubule structures with spindle abnormalities, phenotype, overview
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construction of several chimeras of a tobacco mosaic virus/oilseed rape mosaic virus RdRp chimeric mutant, the R-54k chimera consiting of a hybrid TMV-ORMV RdRp gene, and MP and CP genes of TMV, with an ORMV polymerase domain. Arabidopsis thaliana plants, RLD and Can-0 ecotypes, give nonuniform responses when inoculated with the chimeras
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truncated enzyme forms resulting from deletions of 24, 36, or amino acid residues at the C terminal have RNA-dependent RNA polymerase activity. Truncated enzyme with a deletion of 82 amino acid residues at the C terminal shows no RNA-dependent RNA polymerase activity. Template specificity of the enzyme is not strict wirth NS5B proteins truncated, suggesting that the C terminal of CSFV NS5B protein is involved in the template specificity of the enzyme
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Cystovirus phi6
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structure-based mutagenesis of the enzyme, the elongation rates are not compromised by the mutations, while the transcription rates vary, phenotypes, overview
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rrpC gene knockout by gene disruption
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rrpC gene knockout by gene disruption
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rrpC gene knockout by gene disruption
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construction of D-elp1 protein mutants through (1-1252 aa) and the DELTAC (1-843aa) and DELTAN (844-1252 aa) deletions. D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. D-elp1 depletion results in increased steady state levels of representative transposon RNAs and a decrease in the corresponding transposon antisense transcripts and endo siRNAs. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced
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a mutant is generated as a result of the deletion of a trinucleotide in the N-terminal portion of the coding region, pT7-POL(TRP-). The protein expressed from this mutant lacks a tryptophan residue normally present at the fifth amino acid from the N-terminal glycine. This protein has no detectable enzymatic activity. Mutant pT7-POL(AvII), which lacks the C-terminal 53 amino acids of the normal protein is also inactive
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generation of mutant 3D polymerase plasmids through splicing by overlapping extension PCR. Mutation of the active site of 3D polymerase does not impede its ability to oligomerize or to participate in functional complexes, the catalytically inactive polymerases participate productively in functional oligomer formation and catalysis. But polymerases containing mutations in the amino terminus, which lead to altered contacts in the folded polymerase and mutations in a known polymerase-polymerase interaction in the two-dimensional protein lattice, cannot participate in functional RNA replication complexes
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a hexahistidine affinity-tagged NS5B fusion protein is expressed with recombinant baculoviruses in insect cells
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mutant cm20t in which 7 amino acids in a row are changed to AAASAAA from aa17-23, is totally defective in RNA-dependent RNA polymerase activity
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mutant cm1940t in which 7 amino acids in a row are changed to AAASAAA from aa191-197, is totally defective in RNA-dependent RNA polymerase activity
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mutant enzymes cm2t and cm3t are totally defective in RNA-dependent RNA polymerase activity
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soluble Hepatitis C virus NS5B in the glutathione S-transferase-fused form NS5Bt which lacks the C-terminal 21 amino acid residues, expressed in Escherichia coli. The recombinant soluble enzyme exhibits RNA-dependent RNA polymerase activity in vitro which is dependent on template and primer, but it does not exhibit the terminal transferase activity
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mutant enzyme cm223t in which 7 amino acids in a row are changed to AAASAAA from aa220-226, shows 50% of the activity of the wild-type enzyme
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C-terminal hydrophobic domain deletion mutant, NS5B DELTAC21, shows increased solubility, the deletion also positively affects the polymerase activity
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deletion of only 19 amino acids from the amino terminus severely reduces the polymerase activity, which is completely abolished when 40 amino acids are removed. Truncations from the carboxy terminus are less deleterious
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removal of the C21 domain enhances the enzyme stability. Whereas RNA synthesis by the full-length enzyme remains relatively constant at 12-100 mM KCl, synthesis by DELTA21 truncation mutatnt rapidly decreases at KCl concentrations greater than 12 mM. Binding by DELTA21 mutant but not full-length enzyme decreases proportionally as the KCl concentration increases from 25 to 200 mM. The truncation mutant becomes severely inhibited at elevated NTP concentrations, which most likely is due to competitive binding of the noncomplementary nucleotide to the polymerase catalytic center
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mutant activity analysis by transient replicon assay, overview
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mutant activity analysis by transient replicon assay, overview
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mutant NS5B DELTA21, produced by cells expressing the HCV replicon, shows increased ability to bind to RNA, with 8fold higher affinity compared to the wild-type, in the presence of cyclosporine A, overview. CsA-resistance mutations locate to two functionally related regions in NS5B structure. Purified recombinant NS5B mutants show higher de novo initiated RNA synthesis than the wild-type control
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mutant NS5B DELTA21, produced by cells expressing the HCV replicon, shows increased ability to bind to RNA, with 8fold higher affinity compared to the wild-type, in the presence of cyclosporine A, overview. CsA-resistance mutations locate to two functionally related regions in NS5B structure. Purified recombinant NS5B mutants show higher de novo initiated RNA synthesis than the wild-type control
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impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
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temperature sensitivity of a ts-mutant
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the activity of the 6His-tagged enzyme HRV-16 3D polymerase is identical to HRV-16 3D polymerase without the 6His-tag
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transfection of a mutant icDNA expressing an RdRp lacking the C-terminal disordered domain leads to a drastic reduction in the copy numbers of both forms of viral RNA. This could be due to the loss of interaction between the disordered domain of RdRp and P10 and possibly other viral/host proteins that might be required for the assembly of viral replicase
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transfection of a mutant icDNA expressing an RdRp lacking the C-terminal disordered domain leads to a drastic reduction in the copy numbers of both forms of viral RNA. This could be due to the loss of interaction between the disordered domain of RdRp and P10 and possibly other viral/host proteins that might be required for the assembly of viral replicase
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TMV-induced SlRDR1 expression is blocked by SlAOX1a silencing and enhanced by AOX activator, but SlRDR1 silencing does not influence TMV-induced SlAOX1a activation
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silencing of the transcripts of StRDR1a and StRDR1b by dsRNA hairpin transcripts, expression of silencing constructs for StRDR1 does not affect the expression of the StRDR2 or the StRDR6 genes. Gene silencing does not affect the plant susceptibility to plant viruses, potato virus Y, potato virus X, and tobacco mosaic virus
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silencing of the transcripts of StRDR1a and StRDR1b by dsRNA hairpin transcripts, expression of silencing constructs for StRDR1 does not affect the expression of the StRDR2 or the StRDR6 genes. Gene silencing does not affect the plant susceptibility to plant viruses, potato virus Y, potato virus X, and tobacco mosaic virus
additional information
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construction of several chimeras of a tobacco mosaic virus/oilseed rape mosaic virus RdRp chimeric mutant, the R-54k chimera consisting of a hybrid TMV-ORMV RdRp gene, and MP and CP genes of TMV, with an ORMV polymerase domain. Arabidopsis thaliana plants, RLD and Can-0 ecotypes, give nonuniform responses when inoculated with the chimeras
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construction of an RdRp-defective gRNA mutant
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non-polyadenylated transcripts from a sampling of long-terminal repeat, LTR, retrotransposons are lost in rdr2 mutants
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active-site mutation, GDD -> GAA, in amino acid positions 663 to 665 of NS5 causes the complete loss of NS5 polymerase activity
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active-site mutation, GDD -> GAA, in amino acid positions 663 to 665 of NS5 causes the complete loss of NS5 polymerase activity
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